AUBURN UNIVERSITY

 

1. A.  STANDARD BIOGRAPHICAL DATA

 

Name: Douglas C. Goodwin

 

Department:  Chemistry and Biochemistry              College:  COSAM

 

Present Rank:  Professor                                           Years Completed in Present Rank:  6          

 

Years in Faculty Service at AU:  26                         Years in Faculty Service Elsewhere:  0

 

Type of Current Appointment:  Tenured                  Graduate Faculty Status:  Level 2

 

Pay Basis:  12 month                       

 

                                                                                   

Education:
Institution	Degree	Major	Year Awarded
Utah State University	Ph.D.	Biochemistry	1996
University of Northern Colorado	B.A.	Nutrition	1991

 

 

Professional Experience:
Institution	Rank/Position			Period of Appointment
Auburn University	Ruth W. Molette Professor and Chair			October 2023 - present
Auburn University	Department Chair			July 2020 - present
Auburn University	Professor			August 2019 - present
Auburn University	Associate Professor			August 2005 – July 2019
Auburn University	Assistant Professor			September 1999 - July 2005
Vanderbilt University	Postdoctoral Associate			October 1996 – August 1999

 

 

 

 

 

1. B.  SUMMARY OF ACTIVITIES
Teaching (25%)
Courses Taught while at Auburn ·  SCMH 1010 – Concepts of Science ·  CHEM 1020 – Survey of Chemistry II ·   CHEM 1030 – Fundamentals of Chemistry I ·   BCHE 5180/6180 – General Biochemistry I ·   BCHE 5190/6190 – General Biochemistry II ·   BCHE 7200 – Advanced Biochemistry I ·   BCHE 7220 – Cellular and Molecular Enzymology New Courses Developed while at Auburn ·   BCHE 5180/6180 – General Biochemistry I ·   BCHE 5190/6190 – General Biochemistry II ·   BCHE 7200 – Advanced Biochemistry I ·   BCHE 7220 – Cellular and Molecular Enzymology	Advising (in Career and while at Auburn) ·   Ph.D. completed: 17 as chair; 64 as cmte member (all AU) ·   Ph.D. in progress: 5 as chair; 8 as cmte member (all AU) ·   Masters completed: 0 as chair; 7 as cmte member ·   UG research advisor: Completed 74 (71 AU); Current: 3 ·   HS student research advisor: Completed 4; Current: 1 Teaching/Advising Awards ·   COSAM Outstanding Undergraduate Mentor (2020) ·   Mortar Board Excellence in Teaching (2018) ·   Dean’s Award for Outstanding Advisor (2017) ·   SGA Outstanding Faculty Member (2015) ·   Dean’s Award for Outstanding Teacher (2011) ·   Golden Key Honor Society Teaching Award (2001)
Research (40%)
Research Grants while at Auburn Extramural Sources ·  PI: NSF, ACS Petroleum Research Fund ·  Co-PI: NIH, USDA, BASF   Intramural Sources ·   IGP, CRG, PRISM, COSAM Travel, Auburn Biogrant, Small Instrumentation   ·   Start up funds: $160,000 ·   Other internal funding: $189,120 ·   Total Extramural funding (PI): $1,064,084 ·   Total Extramural funding (co-PI): $1,649,165	Publications (in Career and while at Auburn) Peer-Reviewed Research Publications ·   Journal Articles: Career, 42; Auburn, 28 ·   Proceedings/Book Chapters: Career, 4; Auburn 3 ·   Career Citations: 2886 ·   H index: 27; i10 index: 38   Presentations (in Career and while at Auburn) ·   Invited Talks/Lectures: 36 Career; 31 Auburn ·   Meeting Presentations: Career, 126; Auburn, 111   Selected Advisee Awards while at Auburn ·   Malone-Zallen Fellowship; Distinguished Dissertation Award; CMB Summer GRA
Service and outreach (35%)
Service at Auburn DCB ·  Department Chair ·  Graduate Program Officer/Grad Program Cmte Chair ·  Departmental Leadership Council ·  Graduate Program Assessment Development ·  Biochemistry Division Chair COSAM ·  COSAM Leader selection committees ·  CMB Program Graduate Fellowship Committee ·  Dean Search Committee (2022, 2023) ·  Assoc. Dean Searches (ADR [Chair], ADAA, BMS) University ·  University Senate representative for DCB ·  APA+EP Advisory Council ·  Faculty Comp, Workload, Productivity Advisory Cmte Professional Service ·  NSF reviewer (ad hoc and panelist) ·  Program Chair, 11th Annual SE Enzyme Conference ·  Treasurer: ACS, Auburn Section	·  Reviewer: Proc. Nat. Acad. Sci., J. Am. Chem. Soc., Biochemistry, J. Biol. Chem., J. Inorg. Biochem., PLOS One, Biochim. Biophys. Acta, Biochemie, J. Biol. Inorg. Chem., Chem. Res. Toxicol. Bioorg. Med. Chem., et al.   Outreach at Auburn Sparks STEM prison lecture series ·  Speaker ·  Faculty recruiter/organizer/new-faculty guide   AU Competitive Outreach Grant ·  Co-PI prison education course development   Summer Bridge Program (COSAM) ·  Undergraduate research involvement Q and A ·  Hands-on research demonstration   Outreach Awards ·  COSAM Faculty Service/Outreach Award (2015) ·  ACS Outreach Volunteers of the Year (2014)

2.    PERCENTAGE BREAKDOWN OF DUTIES

 

Teaching, 25%            Research, 40%          Outreach/Service, 35%

 

 

3.  HONORS AND AWARDS

 

Teaching and Advising Awards

 

COSAM Outstanding Undergraduate Mentor Award. College of Sciences and Mathematics, 04/20.

 

Mortar Board Excellence in Teaching Award. Mortar Board National College Senior Honor Society, Sphinx Chapter, Auburn University, 02/18.

 

Dean’s Award for Outstanding Advisor. College of Sciences and Mathematics, 04/17.

 

Student Government Association Outstanding Faculty Member Award. Auburn University, 04/15.

 

Final Lecture Nominee. Student Government Association-sponsored student-nominated award. Finalist selected by campus-wide vote of the students. Auburn University, 02/14.

 

Dean’s Award for Outstanding Teacher. College of Sciences and Mathematics, Auburn University, April 2011.

 

Alpha Epsilon Delta Honorary National Membership. Awarded by the Auburn University AED Chapter, April 2011.

 

Golden Key National Honor Society Teaching Award, Golden Key Honor Society, Auburn University Chapter, April 2001.

 

Outreach Awards

 

College of Sciences and Mathematics Faculty Service/Outreach Award. Auburn University, April 2015.

 

American Chemical Society Outreach Volunteers of the Year. Auburn Section of the American Chemical Society, February 2014.

 

Fellowships, Traineeships, and Academic Awards

 

Center in Molecular Toxicology Postdoctoral Research Trainee, Department of Biochemistry, Vanderbilt University School of Medicine, 07/98 – 08/99.

 

Willard L. Eccles Family Foundation Fellow, College of Science, Utah State University, 10/92- 09/95.

 

E.L. and Inez Waldron Award, Biotechnology Center, Utah State University, 06/96.

 

George Emert Scholar, Chemistry and Biochemistry, Utah State University, 05/96.

 

Thomas F. Emery Memorial Research Scholar, Chemistry and Biochemistry, Utah State University, 05/95.

 

 

4.   SCHOLARLY CONTRIBUTIONS

 

 

4. A.  TEACHING

 4.A.a.  Courses Taught

 

Year	Semester	Course	Title		Hrs	Students
2024	Spring	BCHE 7220		Cellular and Molecular Enzymology	3	8
2023	Fall	BCHE 5190/6190		General Biochemistry II	3a	60
	Spring	BCHE 5190/6190		General Biochemistry II	3a	135
2022	Spring	BCHE 7220		Cellular and Molecular Enzymology	3	6
2020	Spring	BCHE 7220		Cellular and Molecular Enzymology	3	12
2019	Fall	CHEM 7950		Grad Student Orientation Seminar	1	17
	Spring	BCHE 5190/6190		General Biochemistry II	3a	110
2018	Fall	CHEM 7950		Grad Student Orientation Seminar	1	17
	Spring	BCHE 7220		Cellular and Molecular Enzymology	3	14
2017	Fall	CHEM 7950		Grad Student Orientation Seminar	1	25
	Spring	BCHE 5190/6190		General Biochemistry II	3a	96
2016	Fall	BCHE 5190/6190		General Biochemistry II	3a	92
	Spring	BCHE 7220		Cellular and Molecular Enzymology	3	10

^aTwo, two-hour review sessions are offered prior to each exam; Total: 8 sessions/16 hours per semester.

 

Cumulative Teaching Experience at Auburn:

BCHE 7220 Cellular and Molecular Enzymology (10´, 111 students, ~11 per offering)

BCHE 7200 Advanced Biochemistry I (6´, 145 students, ~24 per offering)

BCHE 5190/6190 General Biochemistry II (14´, 1,318 UG/68 G students, ~94/5 per offering)

BCHE 5180/6180 General Biochemistry I (5´, 639 UG/20 G students, ~128/4 per offering)

BCHE 6190 General Biochemistry II (prior to piggyback split) (6´, 488 students, ~81 per offering

CHEM 1030 Fundamentals of Chemistry I (1´, 211 students)

CHEM 1010 Survey of Chemistry II (1´, 119 students)

SCMH 1010 Concepts of Science (2´, 415 students, ~208 per offering)

CHEM 640 (16 students)/CHEM 646 (18 students) (qtrs, 1´ each – roughly eq. to BCHE 7200)

 

 

The number of Biochemistry Division faculty combined with the number of section offerings for the large BCHE 5180/6180 and BCHE 5190/6190 courses has not enabled division faculty to teach outside of the department’s BCHE courses since 2009.

 

I was given release time from teaching in Fall 2017 to support progress on a new NSF grant, and to offset the increase in service commitment starting in Summer 2017 as the DBC Graduate Program Officer (GPO). Organizing and executing the New Graduate Student Seminar (Fall semesters) is part of GPO duties. The necessary tasks include soliciting participating faculty (multiple departments/units on campus), scheduling, generating material and presenting for two of the sessions, and monitoring student attendance. Since taking the position of Chair of the Department of Chemistry and Biochemistry, I have contributed to instruction as needed by the Biochemistry Division.

 

4.A.b.  Graduate students whose work has been completed

 

4.A.b.1. Dr. Goodwin as major professor

Dr. Rejaul Islam, Ph.D. Graduate, Chemistry. December 2024. Dissertation Title: Toward Identification and Evaluation of Multitarget Inhibitors: Targeting Shikimate Pathway Enzymes in Mycobacterium tuberculosis.

 

Dr. Tarfi Aziz, Ph.D. Graduate, Chemistry. December 2022. Dissertation Title: Investigating a novel protein-based cofactor: toward elucidating the catalase mechanism of Mycobacterium tuberculosis KatG. Dr. Aziz is engaged in postdoctoral research in the laboratory of Dr. Kristine Griffett in the Department of Anatomy, Physiology, and Pharmacology in the College of Veterinary Medicine, Auburn University.

 

Dr. Callie Barton, Ph.D. Graduate, Chemistry. December 2022. Dissertation Title: Catalase-Peroxidase: A Structure that Facilitates Electron Transfer, Protein-based Cofactor Formation, and Antibiotic Activation. Dr. Barton is currently a lecturer in the Department of Chemistry and Biochemistry at Auburn University.

 

Dr. Md Jahangir Alam, Ph.D. Graduate, Chemistry, August 2022. Dissertation Title: Evaluation of Bacillus biocontrol potential through the lens of secondary metabolite diversity in genomic, enzymatic, and chemical space. Continuing career as a postdoctoral researcher investigating ultrahigh throughput mass spectrometry using rapid acoustic ejection MS. Dr. Alam will be under the direction of Dr. Paul Harradine and Dr. Kevin Bateman.

 

Dr. Jessica R. Kenneson, Ph.D. Graduate, Chemistry, September 2021. Dissertation Title: Impact of the oxidizable scaffold of catalase-peroxidase (KatG): Modulation of a heme peroxidase for catalytic versatility. Jessica continued her career as a postdoc at Yale University School of Medicine under the direction of Dr. Karen Anderson. She is now a Senior Biochemist with Fermatix in Boston.

 

Dr. Hui Xu, Ph.D. Graduate, Chemistry. Project: August 2020. Dissertation Title:  How an arginine switch promotes the self-preservation of an H₂O₂-degrading enzyme KatG: Strategic use of an active site tryptophan. Dr. Xu continued her career with postdoctoral research at the University of Texas, San Antonio, under the direction of Dr. Aimin Liu, and in April 2022, she moved on to Frontage Laboratories, Inc.

 

Dr. Rene Ngolui Fuanta, Ph.D. Graduate, Chemistry, August 2018. Dissertation Title: Transition from classical methods to new strategies: Mechanistic evaluation of inhibitors against Mycobacterium tuberculosis shikimate kinase. Continued career and currently engaged as a tenure-track faculty member in the Department of Chemistry and Biochemistry at East Stroudsburg University.

Dr. Olive Njuma, Ph.D. Graduate, Chemistry, August 2016. Dissertation Title: Resolving the paradoxical nature of a bifunctional enzyme: Pathways and regulation of intramolecular electron transfer in KatG. Continued career with postdoctoral research at Vanderbilt University School of Medicine under the direction of Dr. F. Peter Guengerich. Currently employed with Molecular Assemblies, Inc., San Diego, CA.

Dr. Haijun Duan, Ph.D. Graduate, Chemistry, December 2014. Dissertation Title: KatG as a defense against hydrogen peroxide toxicity: from a redundant C-terminal domain to the paradoxical synergy of two mutually antagonistic activities. Continued career in postdoctoral research, first at the University of Kentucky under the direction of Dr. Anne-Frances Miller, and currently in the Structural Biology Unit of the Van Andel Institute in Grand Rapids, MI. He is under the direction of the Program Lead, Dr. Huilin Li.

Dr. Elizabeth Ndontsa, Ph.D. Graduate, Chemistry, May 2013. Dissertation Title: Synergy not antagonism in antioxidant defenses: the unanticipated effect of electron donors on catalase-peroxidase function. (*AU Distinguished Dissertation Award) Continued career as a postdoctoral research associate at Scripps Research Institute and University of California, Berkeley under the direction of Michael Marletta. Currently employed as a Project Manager at Gilead Inc., Berkeley, CA.

 

Dr. Yu Wang, Ph.D. Graduate, Chemistry, December 2012. Dissertation Title: Gene duplication and fusion: Strategy for active-site control and starting point for new catalysts. Continued career as a postdoctoral researcher at Virginia Tech under the direction of Dr. Robert White. Became a tenure-track faculty member at University of North Georgia and was promoted with tenure to associate professor before electing to pursue an MD at Morehouse Medical School in Atlanta, GA.

 

Dr. Shalley Kudalkar, Ph.D. Graduate, Chemistry, May 2012. Dissertation Title: Roles of Large Loops in Catalytic Versatility of Catalase-Peroxidases: Significance of Peripheral Structures in Improvising Enzyme Functions. Continued as a postdoc at Vanderbilt University (Dr. Lawrence J. Marnett), then as a Associate Research Scientist at the Yale School of Medicine. Currently, a Senior Research Scientist at Merck.

 

Dr. Robert Moore, PhD Graduate, Chemistry, May 2009. Dissertation Title: Toward the Understanding of Complex Biochemical Systems: The Significance of Global Protein Structure and Thorough Parametric Analysis. Continued career as an adjunct faculty member in the Department of Chemistry at Wayland Baptist University. He is currently a tenured full professor in that department.

 

Dr. Carma Cook, PhD Graduate, Chemistry, May 2009. Dissertation Title: Role of Distant Intrasubunit Residues in Catalase-peroxidase Catalysis: Tracing the role of gene duplication and fusion in enzyme structure and function. Continued career in postdoctoral research at Auburn University, Montgomery. Currently engaged as an Assistant Professor of Chemistry at Chattanooga State Community College.

 

Dr. Ruletha Baker, Ph.D. Graduate, Chemistry, December 2006. Dissertation Title: Roles of an ‘Inactive’ Domain in Catalase-Peroxidase Catalysis: Modulation of Active Site Architecture and Function by Gene Duplication.

 

Dr. Cornelius Varnado, Ph.D. Graduate, Chemistry, August 2006. Dissertation Title:  Enhancing Expression of Recombinant Hemoproteins: Progress Toward Understanding Structure/Function and Therapeutic Application. Continued career in postdoctoral research at Rice University under the direction of Dr. John Olsen. Currently engaged as a Senior Biologic Process Engineer at Allsource/Merck.

 

Dr. Yongjiang Li, Ph.D. Graduate, Chemistry, December 2005. Dissertation Title: Roles of Two Interhelical Insertions in Catalase-Peroxidase Catalysis: Tracing the Impact of Peripheral Protein Structures on Heme Enzyme Function. Continued career in postdoctoral research at the National Institutes on Aging at NIH and then as a Research Associate at the Scripps Research Institute. Presently is a Research Scientist in Research and Development at ScienCell Research Laboratories, Inc., San Diego, CA.

 

Dr. Ronald Marcy, GND Graduate Student, Chemistry, Fall 2002 – Spring 2003. Project: Structure and function of catalase-peroxidases. As an instructor at Alabama Southern Community College, Ron worked weekends in the laboratory to get exposure to the latest techniques in biochemistry and molecular biology in order to enhance teaching of his chemistry and microbiology courses.

 

4.A.b.2. Dr. Goodwin as advisory committee member

 

Student	Degree/Year		Discipline	Advisor
Theo Dusabamahoro	PhD	2024	Chemistry	Dr. E. Duin
Andresa Bezerra	PhD	2024	Chemistry	Dr. C. Easley
Kabre Heck	PhD	2024	Drug Discovery Devel	Dr. A. Calderón
Alex Saundersb	-	2023	Chemistry	Dr. C. Goldsmith
Chidinma Lucy Odili	PhD	2023	Chemistry	Dr. Mansoorabadi
Tingting Qu	PhD	2023	Chemistry	Dr. J. Harshman
Fnu Ibitsam	PhD	2023	Drug Discovery Devel	Dr. A. Kisselev
Kenny Nguyen	PhD	2023	Chemistry	Dr. Mansoorabadi
Shadi Yavari	PhD	2022	Chemistry	Dr. E. Duin
Katherine Clohan	PhD	2022	Chemistry	Dr. E. Duin
Bryan Croninb	-	2021	Chemistry	Dr. E. Duin
Jamonica Moore	PhD	2022	Chemistry	Dr. C. Goldsmith
Chioma Helen Alohc	-	2021	Chemistry	Dr. H. Ellis
Shruti Somaic	-	2021	Chemistry	Dr. H. Ellis
Shuxin Li	PhD	2021	Chemistry	Dr. Mansoorabadi
Qi Cui	PhD	2021	Chemistry	Dr. J. Harshman
Trey Slaneyb	-	2021	Chemistry	Dr. Mansoorabadi
Kara Johnson	PhD	2020	Chemistry	Dr. B. Merner
Richard Hagen	PhD	2020	Chemistry	Dr. H. Ellis
Katie Tombrello	PhD	2019	Chemistry	Dr. H. Ellis
Ahmad Almalkia	PhD	2019	Drug Discovery Devel	Dr. R. Clark
Carly Engel	PhD	2019	Chemistry	Dr. E. Duin
Victoria Owens	PhD	2019	Chemistry	Dr. Mansoorabadi
Claire Graham	PhD	2018	Chemistry	Dr. H. Ellis
Kaiyuan Zheng	PhD	2018	Chemistry	Dr. Mansoorabadi
Juan Hu	PhD	2018	Chemistry	Dr. C. Easley
Dianna Forbes	PhD	2018	Chemistry	Dr. H. Ellis
Younis Abiedallaa	PhD	2018	Drug Discovery Devel	Dr. R. Clark
Marike Vissera	PhD	2018	Veterinary Medicine	Dr. D. Boothe
Jonathan Musila	PhD	2017	Chemistry	Dr. H. Ellis
Selamawit Ghebreamlak	PhD	2016	Chemistry	Dr. E. Duin
Lizette Gomez Ramosb	-	2015	Chem Eng (Ga Tech)	Dr. A. Bromarius
Jiansheng Huang	PhD	2015	Drug Discovery Devel	Dr. P. Panizzi
Andrew Damiania	PhD	2015	Chemical Engineering	Dr. J. Wang
Paritosh Dayalb	-	2015	Chemistry	Dr. H. Ellis
Divya Prakash	PhD	2014	Chemistry	Dr. E. Duin
Johayra Simithya	PhD	2014	Drug Discovery Devel	Dr. A. Calderón
Qiao Zhang	PhD	2014	Chemistry	Dr. C. Goldsmith
Brian Ferguson	PhD	2014	Kinesiology	Dr. B. Gladden
Catherine Njeri	PhD	2014	Chemistry	Dr. H. Ellis
Matthew Barberio	PhD	2013	Kinesiology	Dr. D. Pascoe
Xiao Xiao	MS	2013	Chemistry	Dr. E. Duin
John “Mick” Robbins	PhD	2012	Chemistry	Dr. H. Ellis
Ann Johnsona	PhD	2012	Nutrition	Dr. S. Gropper
Jingyuan Xiong	PhD	2012	Chemistry	Dr. H. Ellis
Chengdong Huang	PhD	2011	Chemistry	Dr. S. Mohanty
Alejandro Silva	MS	2011	Animal Sciences	Dr. F.F. Bartol
Weiya Xu	PhD	2010	Chemistry	Dr. E. Duin
Jody Burke	PhD	2010	Animal Sciences	Dr. J. Wower
Erin Imsand	PhD	2009	Chemistry	Dr. H. Ellis
Russell Carpenter	PhD	2008	Chemistry	Dr. H. Ellis
Matthew Goodwin	PhD	2008	Kinesiology	Dr. B. Gladden
Mi Wang	PhD	2008	Chemistry	Dr. E. Duin
Weikuan Li	PhD	2008	Chemistry	Dr. S. Schneller
Sidharth Venkatesh	PhD	2008	Chemical Engineering	Dr. M. Byrne
Xuanzhi Zhan	PhD	2008	Chemistry	Dr. H. Ellis
Rajesh Gupta	PhD	2008	Chemical Engineering	Dr. Y.Y. Lee
Na Yang	PhD	2007	Chemistry	Dr. E. Duin
Angelo Karavolosb	-	2007	Polymer/Fiber Eng	Dr. Abdel-Hady
John-Ryan McAnnally	MS	2007	Biomedical Sciences	Dr. J. Bradley
Dolapo Adediji	PhD	2007	Chemistry	Dr. E. Duin
Benlian Gao	PhD	2006	Chemistry	Dr. H. Ellis
Honglei Sun	MS	2006	Chemistry	Dr. H. Ellis
Ling Tang	PhD	2006	Animal Sciences	Dr. W. Bergen
Wei Ye	PhD	2005	Chemistry	Dr. S. Schneller
Chunru Linb	-	2005	Biological Sciences	Dr. M. Wooten
Rong Wu	PhD	2005	Chemistry	Dr. S.D. Worley
Darcy Goodwin	MS	2004	Animal Sciences	Dr. F.F. Bartol
Amanda Bean	PhD	2004	Chemistry	Dr. T. Albrecht
Ben Stronach	MS	2001	Animal Sciences	Dr. W. Bergen
Wendy White	MS	2001	Biological Sciences	Dr. M. Wooten
aDenotes service as University Reader bStudent resigned prior to completing degree program cStudent transferred to a PhD program at another university

 

4.A.c.  Graduate students whose work is ongoing

 

4.A.c.1. Dr. Goodwin as major professor

 

Chidozie Ugochukwu, Ph.D. Candidate, Chemistry. Co-directed with Dr. Holly Ellis of the Department of Biochemistry and Molecular Biology at the Brody Medical School, East Carolina University. Evaluating the regulatory and metabolic links between sulfur acquisition and metabolism and defenses against reactive oxygen species.

 

Nana Quansah, Ph.D. Candidate, Chemistry. Investigation of biosynthetic gene clusters (BGCs) from the genomes of plant-growth promoting Bacillus species. A particular focus of the project seeks to elucidate the roles cytochromes P450 embedded key Bacillus BGCs.

Sara Collins, Ph.D. Student, Chemistry. This project focuses on catalase-peroxidase (i.e., KatG) structure and function. Attention is focused on elucidating critical intermediates in the novel catalase mechanism of KatG, and on identifying intermediates and reactions involved in the establishment of the unique Met-Tyr-Trp protein-based cofactor used by the enzyme.

 

Macee Glick, Ph.D. Student, Chemistry. Production and properties of secondary metabolites produced from the biosynthetic gene clusters (BGC’s) of plant-growth promoting Bacillus species.

 

Jahbo Love, Ph.D. Student, Chemistry. Pursuing the shikimate pathway to develop multi-target inhibitors as leads for antibiotic development against Mycobacterium tuberculosis. The project focuses on structural characterization of enzyme-inhibitor complexes (shikimate dehydrogenase and shikimate kinase) using x-ray crystallography, ¹⁹F-NMR, and intrinsic protein fluorescence.

 

4.A.c.2. Dr. Goodwin as committee member

                       

Student	Degree (L)a	Discipline	Advisor
Prosenjit Ray	PhD (C)	Chemistry	Dr. Mansoorabadi
Chelsea Rand	PhD (C)	Chemistry	Dr. Mansoorabadi
Arielle Dallas	PhD (C)	Chemistry	Dr. E. Duin
Chukwuemeka Okpala	PhD (C)	Chemistry	Dr. E. Duin
Harun Abdullah	PhD (C)	Chemistry	Dr. R. Banerjee
Laura Hall	PhD (S)	Chemistry	Dr. Katie Rush
Dakota Grimes	PhD (S)	Chemistry	Dr. R. Banerjee
Farouq Busari	PhD (S)	Chemistry	Dr. Katie Rush
aL – Level, designates current progress toward degree. C – PhD candidate; S – PhD student

4.A.cc  Undergraduate Student Research Supervised (Current in italics):

 

Student	Major	Dates	Fellowships
Erin Wilkinson	Biochemistry	08/25 – present	Marks
Amy Lee‡	-	02/24 – present
Jada Conner	BA Chemistry	01/24 – present	AU URF, Marks
Louisa Forbes	Biochemistry	08/23 – present	Marks
Danny Oh‡	-	05/25 – 8/2025
Elizabeth Wall	Bus. (Pre-Med)	08/23 – 5/25
Braeden Olson	Biomed Sci	01/23 – 5/24
Reilly Bass	Biochemistry	08/23 – 12/23
Ryan Mumford	Biochemistry	08/21 – 5/23	Marks
Nina Orihuela	BA Chemistry	08/21 – 5/22	Marks
Benjamin Faulkner	Chem Eng	01/21 – 5/22
Madeleine Forbes	Chemistry	08/20 – 11/21
Raegan Gantt	BA Chemistry	01/21 – 04/21
Monty Greene†	BA Chemistry	01/21 – 04/21
Aishah Lee	Biochemistry	05/19 – 08/21	NSF, Marks
Laura Minton	Biomed Sci	03/19 – 05/20	Marks
Melissa Williams	Biochemistry	05/19 – 12/19
Daniel Bayer	BA Chemistry	03/19 – 07/19
Savannah Petrus	Biochemistry	01/18 – 05/19	Marks
Patrick Sahrmann	Biochemistry	08/16 – 05/19	AU URF, Marks
Kirklin McWhorter	Biochemistry	05/17 – 12/18	CMB, Haggard
Michael Skinner	Biomed Sci	01/15 – 12/17	CMB
Olivia Snider	Biochemistry	05/15 – 05/16	CMB, Marks
Theresa Simermeyer	Biochemistry	05/15 – 05/16
Daniel Zieman	BA Chemistry	08/15 – 10/15
Moneisha Cunningham	BA Chemistry	01/15 – 06/15
Alex Kollhoff	Biomed Sci	05/14 – 02/15	CMB
Lauren Barr	Biomed Sci	01/14 – 05/15	Marks
Teddy Childers	Biomed Sci	01/14 – 12/14
Ethan McCurdy**	BA Chemistry	01/13 – 06/14	AU URF
Gobind Gill*	Biochemistry	06/12 – 06/14	CMB
R. Elliot Browning	Biomed Sci	01/13 – 12/13
Jennifer Lewis	Biomed Sci	06/12 – 05/13
Benjamin Jackson	Biomed Sci	05/11 – 05/12
Jordan Suh	Chemistry	01/11 – 05/12	CMB
Kristen Henninger	Chemistry	09/10 – 05/11
Kendall Walton	Chemistry	09/10 – 05/11
Sara Ransom*	Biomed Sci	05/10 – 05/11	CMB
Thomas Townes	Biomed Sci	09/10 – 12/10
Ryan Tucker	Biochemistry	09/09 – 07/10
John Pribonic	Biochemistry	05/09 – 07/09
Michael Dumas	Biomed Sci	05/09 – 09/09
Corey Prescott	Chemistry	01/09 – 05/09
Robert Campbell	Biochemistry	05/08 – 05/09	CMB
JaRyce Nabors	Biochemistry	08/07 – 05/08
Michelle Muldowney	Biochemistry	08/07 – 12/08
Joey Russell	Biomed Sci	01/08 – 05/08
Rachel Williams	Biochemistry	01/07 – 12/07
Jessica Williams	Biochemistry	05/07 – 08/07
Michael Love	Chemistry	01/07 – 12/07
Alex Taylor	Biochemistry	08/06 – 12/06
John-Ryan McAnnally	Biomed Sci	01/06 – 12/06
Luke Powell	Biochemistry	08/05 – 12/06	COSAM URF
JaRyce Nabors	Biochemistry	05/06 – 08/06	EPSCoR
Jennifer Smith	Biochemistry	01/06 – 05/06
Allan Bagget	Biomed Sci	01/06 – 05/06
Kimberley Laband	Molecular Biol	05/03 – 05/05	AU URF
Dan Carter	Biomed Sci	09/-04 – 12/04
Byron Smith	Biomed Sci	08/04 – 12/04
Shawn Pugh	Biomed Sci	05/04 – 08/04
Stephen Pehler	Molecular Biol	04/04 – 11/04
Tyson Kilpatrick	Biomed Sci	01/04 – 05/04
Greyson McGowin	Biomed Sci	05/03 – 09/03	CMB
Derek Fortson	Biochemistry	09/02 – 05/03	COSAM URF
J. Kenneth Roberts	Biomed Sci	06/02 – 05/03
Sarah Peaslee	Biochemistry	06/02 – 05/03
Melanie Oliver	Microbiology	05/02 – 12/02
Robert Thomas	Asbury College	05/02 – 09/02
Kristin Hertwig	Biochemistry	01/00 – 12/02	AU URF
Erika Schansberg	Microbiology	09/01 – 05/02
Thomas Cash	Chemistry	01/02 – 05/02
Matthew McIntyre	Biomed Sci	05/01 – 09/01
Nancy Ruth Wilkins	Biochemistry	05/01 – /09/01
Emily Brantley	Molecular Biol	06/00 – 12/01
Juan Carmona	Molecular Biol	09/00 – 05/01
Amy Wainwright	Biochemistry	01/00 – 06/00
Randy Bootha	Biochemistry	05/96 – 09/96
Joseph Bensona	Biochemistry	05/95 – 05/96
Curtis Takemotoa	Political Sci	05/94 – 05/96
**Dean’s Undergraduate Research Award (2013 – 2014); NSF GRFP recipient at Columbia University *Honors Thesis completed based on Goodwin laboratory research †CHEM 2980 requirement filled by DCB Colloquium; DCG managed assignments and evaluation ‡Auburn City High School Student aResearch completed at Utah State University

 

 

4.A.d.  Courses and curricula developed

 

At the time I came to the Department of Chemistry and Biochemistry (DCB), I was the only research-active biochemist, the first of a new generation of biochemistry faculty. I was charged with building a division of biochemistry for the future of the DBC. Coincident with this, Auburn University changed from quarters to semesters, and the BCHE heading and its entire panel of courses came into existence. Consequently, every course I taught required the development of a course essentially from scratch.

 

The General Biochemistry Sequence: BCHE 5180/6180 and BCHE 5190/6190. As a two-semester biochemistry course requiring a prerequisite full year of sophomore organic chemistry, this course is intended to build an understanding of metabolism (broadly defined) from a structure and mechanism perspective. This includes not only the small-molecule level of metabolites and the catalyzed reactions that result in their chemical transformations, but also macromolecular structure and mechanism of enzymes, other proteins, nucleic acids, etc. With this in mind, the general organization of the course is to build and understand the large majority of biological catalysts (i.e., enzymes) by building them from the ground-up (i.e., amino acid structure/properties to protein structure/properties to principles of catalysis). From there, metabolism is addressed starting with core pathways like the citric acid cycle and respiratory electron transport. Thereafter, the course unfolds as alternating units of structure – metabolism – structure – metabolism, etc.). For example, units on lipid structure are immediately followed by lipid metabolic pathways and so on. In support of this, I have generated a large library of my own custom-made protein and other structural images. I use these tailor-made images to show the structures/mechanisms and illustrate the principles of the course. This is supported by the vast array of protein structural data now available in the protein data bank (PDB) and software (e.g., PyMol) for generating clear, compelling images of biological macromolecules. In addition to providing powerful visual tools to illustrate the principles of the course, it enables me to share with students information from the most recently solved structures for a given topic, keeping well ahead of the pace afforded by the typical biochemistry textbook. Indeed, I no longer require a traditional textbook for the course. Finally, to foster student engagement of the material, I have incorporated active participation exercises for students. Some are technology-based (e.g., smartphone-based polling, etc.), and others are decidedly “low tech” such as constructing metabolic maps from regulatory information and having students help me act out enzyme and other mechanisms in the Molecular Players Theater.

 

Advanced Biochemistry I: BCHE 7200. This course was developed along the same principles as for the General Biochemistry sequence above. However, there are two additional challenges presented by the course in that it must have similar topic coverage over one semester rather than two, and the course is taken by a diverse cohort of students whose backgrounds in chemistry and biology are highly varied. As such, the course includes content in the early sessions to provide some general background in these areas to support subsequent course content.

 

Principles of Cellular and Molecular Enzymology: BCHE 7220. This course centers on two main types of questions, each covering about half of the course. The first type centers on the “how” of enzyme catalysis: How do enzymes work, or how does catalysis work from within the context of an enzyme active site? How are specific kinds of reactions catalyzed by enzymes? That is, what are the functional groups provided by an enzyme, and how do they facilitate specific reaction steps? The second half of the course answers the question: How does one investigate enzyme catalysis? What are the techniques and what data are collected? How are the data analyzed and interpreted? The theoretical framework and the examples that illustrate the principle points of the course are from the current literature. So, though the framework of the course remains the same, it is continually keeping abreast of current developments. The course calls on students to evaluate and present specific enzyme assays, enzyme cofactors, and mechanistic advances from the primary literature. The most recent iteration of the course was taught in an EASL environment in the Mell classroom building. Student teams used PyMol software in class to build images of enzymes from new structures reported in papers under discussion. Likewise, students were introduced to KinTek Global Explorer software to evaluate enzyme kinetic models. This allows students to observe anticipated enzyme reaction outputs for a given mechanistic model and to pick specific parameters and observe how continuously scrolling their values up or down influences that output. This helps to illustrate the difference between proposed steps in a mechanism that are constrained by available experimental data and those that are not. As such, students have a valuable tool from which to propose new experiments to address mechanistic steps in the latter category.

 

 

4.A.g.  Other contributions to teaching

 

Peroxidase demonstration development. The activity of peroxidase enzymes is particularly striking demonstrations for teaching (here) and outreach (see 4.C.a Commentary) The turnover of these enzymes in the presence of hydrogen peroxide is detected by the oxidation of a variety of compounds to free radical products. With particular substrates, the radicals generated are stable and easily observed based on their intense colors (blue, pink, green, purple, yellow, etc.). Further, the addition of ascorbate (vitamin C) reduces all of these radicals at diffusion-controlled rates returning solutions to a clear state. I have capitalized on these visually striking phenomena to produce demonstrations on redox titration (Fundamentals of Chemistry I), light absorption (Concepts of Science), enzyme catalysis and kinetics, and antioxidant properties of vitamins (Summer Bridge Program, see Outreach, 4.C.a Commentary). The versatility of this system allows for tailoring demonstrations education or outreach audiences ranging from middle school to undergraduates.

           

            Undergraduate/Graduate Student Seminar Assessment Instrument. In order to facilitate assessment of students giving talks in Division of Biochemistry seminars, I adapted an enhanced rubric to guide evaluators in assessing six components of an effective scientific presentation (scientific significance, introduction, knowledge of subject, clarity of presentation, quality of visual aids, and quality of presentation). Included with the rubric are scaled descriptions of the characteristics that merit Likert scale scores of 1 – 5 in each category. This has since been adopted department-wide and applied to students registered for Undergraduate Seminar (CHEM 4950) and Formal Presentations in Modern Chemistry (CHEM 7750). Similarly, I have produced additional rubrics as instruments to assess various aspects of our department’s graduate programs (see Department of Chemistry and Biochemistry Service 4.D.a.1).

 

4.A.h.  Statement of Teaching Philosophy

 

My teaching philosophy starts with the inescapable fact that teaching is intensely relational. It is a great privilege and grave responsibility. As a teacher-scholar, it is essential that I recognize that I am likely to be one of only a couple or even the sole ambassador of my field to my students. Consequently, as the students who pass through my classes graduate and progress through the next stages of their lives, how they view biochemistry will be heavily influenced by their experience in my course. As such, it is my goal that students engage and investigate biochemistry deeply and that the opinions they form about it have little to do with me and everything to do with the material we investigate. Thus, I operate by the maxim “the closer you look, the better it gets”. In the natural world, a closer look reveals a more fascinating and elegant universe than could possibly be imagined from a simple cursory investigation.

 

My aim is to draw my students’ attention to the intricate operations of the molecules of living organisms at a structural level in two ways. First, in terms of the mechanisms of the reactions involved, biology employs recognizable chemical strategies across multiple contexts; understanding these strategies in one pathway sheds light on their application in other areas of metabolism. Second, in terms of the macromolecules involved (e.g., enzymes, receptors, etc.), an explosion of structural data available in the protein data bank (PDB) enables me to prepare and show custom images of these molecules (often in multiple conformational states); the student can come away with a much clearer idea about how these things work. Indeed, I have done this to such an extent that I now no longer require a traditional textbook for any of the biochemistry courses I teach. Importantly, details are not just given for details’ sake, but to extend to the larger picture of inter-cell and inter-tissue communication and coordination with application to normal and pathophysiological conditions.

 

I endeavor to foster student engagement of the material on many levels. The first and simplest is to be unapologetically and unabashedly enthusiastic about the material. Because it is a virtual certainty that every student’s enthusiasm for the subject will come in below mine, my setting the bar low (i.e., unenthused) in this respect will create a dreadful classroom environment. This is not “cheerleading” but merely taking the time to point out for students what about the material is remarkable. I am aided greatly in the volume of structural data mentioned above. I am able to bring the subject alive to students in a way that was impossible only a handful of years ago. At the next level, I frequently poll students (by a variety of methods) to identify misconceptions (prior to content coverage) and to evaluate the level of understanding (following content coverage). Above this, I have students, as a group, take a set of data and use it to predict a physiological outcome. For example, from a cell/tissue type and a physiological state (e.g., fight-or-flight), they work to predict the regulatory impacts on individual enzymes, and from there, draw a metabolic map showing the flow of major cellular metabolites. Finally, I engage the class in the Molecular Players Theater. In this, students are volunteered to assist in literally acting out mechanisms that are difficult to understand.

 

As a result of efforts centered on this approach, it is my expectation that students will be able to test above the level of simple multiple choice and true/false. I expect that students will be able to apply the concepts and principles imparted through our activities to synthesize reasonable solutions to new problems. Simply stated, memorization is an invaluable skill that certainly aids in the generation of creative solutions to confounding problems. However, simple regurgitation of facts does not demonstrate an ability to apply a sharp memory, and as such, will not be sufficient to excel in my courses. Here the interpersonal and relational nature of teaching manifests itself as well. Ultimately, I believe it is important to pay our students the compliment of high expectations. Praise of the high quality of our students is often spoken, but it rings hollow if we never push our students to excel to the level of their capabilities. Time and again I have demanded much from my students. Far more often than not, they themselves are gratified to discover what they can achieve.

Finally, due to its intensely interpersonal nature, I believe that optimal teaching effectiveness can only be achieved if I place the best interest of the students above my own. While this is easy to say or write, carrying it out as a teaching philosophy is much more difficult. There are no shortcuts. For students to believe that an instructor cares about them, that teacher must truly care about their educational needs, aspirations, and difficulties. Likewise, for students to believe that an instructor is available and approachable, that teacher must commit to making time for students and creating an atmosphere that encourages questions and discussion. By combining the practical approaches that maximize student interest and participation with the personal commitment of the teacher to the best interests of the students, I believe that a rich and rewarding learning environment can be created for both teacher and students.

 

           

4. B. RESEARCH

 

4.B.0   Description of Research Program  

 

            Goodwin laboratory student success. An important measure of the success of this research program is the students who have contributed to its progress over years. Following the completion of their degrees (see 4.A.b.1 Dr. Goodwin as major professor), they have gone on to postdoctoral positions at some of the top institutions and labs in the country, including the National Institutes of Health, the Scripps Research Institute, Vanderbilt, Yale, Berkeley, Rice, University of Kentucky, Virginia Tech, Merck, and others. Several of my former students have since taken tenure-track faculty positions, and others have moved into positions in industry.

 

The Goodwin Laboratory has three principal interest areas: 1) Catalase-peroxidase (KatG) structure and mechanism, 2) inhibition of shikimate pathway enzymes, and 3) antimicrobial compounds generated by Bacillus and Paenibacillus biosynthetic gene clusters (BGCs).The themes which tie these three research areas together are: bacterial and fungal virulence, antibiotic resistance, and discovery of new leads for antibiotic development. With respect to potential applications, we consider a truly broad range of target organisms from human pathogens like Mycobacterium tuberculosis and Yersinia pestis to pathogens of substantial agricultural concern like Fusarium graminearum, Magnaporthe grisea, and Globisporangium ultimum.

 

Catalase-peroxidase (KatG) Structure and Mechanism. This is the longest standing research area of the Goodwin Laboratory. The KatG enzyme is a truly rich system to evaluate the connections between enzyme structure and mechanism, including mechanisms of cofactor maturation, catalysis, inhibition, and irreversible inactivation. The primary function of KatG is to degrade hydrogen peroxide (H₂O₂). Interestingly, in Mycobacterium tuberculosis (Mtb), KatG is also critical for the activation of the front line antitubercular agent isoniazid. Indeed, it has been estimated that over 70% of isoniazid resistant Mtb carry mutations that render KatG unable to catalyze isoniazid activation. Second, KatG is prominently distributed among some of the planet’s most notorious pathogenic organisms where its production is often connected with other virulence factors. This is true for both bacterial pathogens (e.g., the organisms that causes of tuberculosis and bubonic plague) and fungal pathogens (e.g., the organism that causes rice blast disease). This is expected given that a near universal response of higher eukaryotes (the intended hosts for these pathogens) is to produce large amounts of H₂O₂ to defend against infection.

 

KatG contains multiple novel structural features which produce unprecedented reaction intermediates and mechanisms for self-preservation in the face of the harsh and highly oxidizing environments produced by host immune/defensive responses. A protein-based cofactor containing covalently linked methionine, tyrosine, and tryptophan side chains (the MYW cofactor) is found nowhere else in nature and contributes to an entirely novel mechanism for rapidly disposing of H₂O₂. KatG is also equipped with multiple electron-transfer pathways to diffuse enzyme suicidal intermediates and preserve KatG’s vital function for the pathogens who carry it. Finally, a pH-controlled, conformationally dynamic arginine switch enables KatG to control and direct through-protein radical transfer to maximize enzyme activity and longevity.

 

Identifying inhibitors of Mtb shikimate pathway enzymes. Drug-resistant Mtb continues to pose a substantial threat to human health. Alarmingly, the FDA has only approved a couple of new antitubercular agents since the 1960’s. Clearly, the need for new drugs to treat Mtb is pressing. Collaborating with Dr. Angela Calderón in the Drug Discovery and Development, we are investigating the shikimate pathway as a potential target for new antitubercular agents. We have drawn on natural products as well as computational resources to identify new scaffolds for the development of such compounds. With the former, we have evaluated marine natural products and have identified a derivatized manzamine (6-cyclohexamido-manzamine A) as a potent, slow-binding Mtb shikimate kinase (MtSK) inhibitor. Toward the latter, we have focused on compounds which may be effective dual-target inhibitors against Mtb shikimate dehydrogenase (MtSDH) and MtSK. We have identified a panel of leads, and we are applying X-ray crystallography, ¹⁹F-NMR, tryptophan-based fluorescence, and enzyme kinetic methods to determine inhibition mechanisms and inform strategies to maximize the effectiveness of these compounds.

 

Bacillus and Paenibacillus BGCs. Many Bacillus and Paenibacillus species produce a structurally diverse set of so-called secondary (2°) metabolites; many of these compounds inhibit the growth of root-associated pathogens. As such, these bacteria and the compounds they generate hold exceptional promise for protection of globally essential agricultural products. Secondary metabolism encompasses the production of organic compounds that are not strictly essential for the moment-to-moment survival of cells but often do impart novel properties that enable an organism to occupy a particular ecological niche. Invariably, the series of enzyme activities necessary for producing these metabolites are encoded in biosynthetic gene clusters (BGCs). Different types of BGCs give rise to different classes of secondary metabolites, including polyketides, non-ribosomal peptides, ribosomally-synthesized post-translationally modified peptides, and others. Within classes there is substantial variation, often depending on the specific identity and arrangement of modules which compose a given BGC.

 

Many Bacillus species carry multiple BGCs of various classes. Very often, the 2° metabolites generated from them have antibiotic properties against bacteria, fungi, and/or oomycetes. In collaboration with the Liles and Noel laboratories, we are evaluating the antibiosis properties (breadth of organisms inhibited, potency of inhibition, etc.) of many hundreds of Bacillus and Paenibacillus strains spanning multiple species. From genome sequence data, we identify the BGCs encoded within each strain. We extract metabolites from active cultures, evaluate their antibiotic properties, and use metabolomic tools (e.g., LC-MS/MS) to identify and characterize these compounds. Strains from B. velezensis are particularly prolific in the production of 2° metabolites, and the compounds that many of them generate give rise to broad spectrum abilities to inhibit notorious agricultural pathogens, including Phytophthora nicotianae, Rhizoctonia solani, G. ultimum, and F. graminearum, etc.

 

 

4.B.b.  Article-length publications

 

4.B.b.1. Peer-Reviewed Journal Articles:

(from Google Scholar: h-index = 27; i10 index = 38; total citations = 2886)

(Citations as of 05/12/2025; unless otherwise indicated, 2024 Impact Factors [2024 IF] are shown)

(For all Auburn-based output, *denotes graduate student coauthor; ** denotes undergraduate coauthor)

 

Resulting from research at Auburn University after tenure

 

44.    *Ugochukwu, C. G., Schwartz, T. S., Zeczycki, T. N., Goodwin, D. C., and Ellis, H. R. 2025. Sulfur starvation induces an Fe-replete response and attenuates virulence pathways in Pseudomonas aeruginosa PAO1. (in preparation).

 

43.    *Alam, J., *Olofintila, O. E., *Moen, F. S., Noel, Z. A., Liles, M. R., and Goodwin, D. C. 2024. Broad antibiosis activity of Bacillus velezensis and Bacillus subtilis is accounted for by a conserved capacity for lipopeptide biosynthesis. Frontiers Microbiol. (in press). (2024 IF: 4.5; Times Cited: 0; Goodwin Laboratory Contribution: 70%).

 

42.    Li, J., Duan, R., Traore, E. S., Davis, I., Nguyen, R. C., Goodwin, D. C., Lamb, A., Jarzecki, A. A., Liu, A. 2024. Decoding MYW-OOH: Indole-(N)-linked hydroperoxyl modification modulating Mycobacterium tuberculosis KatG function. Angew. Chemie 63, e202407018. (2024 IF: 16.1; Times Cited: 3, Goodwin Laboratory Contribution: 10%).

 

41.    *Xu, H., *Kenneson, J. R., **Minton, L. E., and Goodwin, D. C. 2024. A switch and a failsafe: KatG’s mechanism for preservation of catalase activity using a conformationally dynamic Arg and an active-site Trp. Frontiers Chem. Biol. 3, 1431412. (2024 IF: 3.8; Times Cited: 0; Goodwin Laboratory Contribution: 100%) (invited contribution)

 

40.    *Basak, S., *Alam, J., Goodwin, D., Harris, J., Patel, J.D., McCullough, P., and McElroy, J.S. 2022. Detecting ACCase-targeting herbicides effect on ACCase activity utilizing a malachite green colorimetric functional assay Weed Sci., 70, 14 – 19. (2020 IF: 2.713; Times Cited: 5; Goodwin Laboratory Contribution: 20%.)

 

39.    de Faria, C. F., Moreira, T., Lopes, P., Costa, H., *Krewall, J. R., *Barton, C. M., Santos, S., Goodwin, D. C., Mochado, D., Viveiros, M., Machuqueiro, M., and Martins, F. 2021. Designing new antitubercular isoniazid derivatives with improved reactivity and membrane trafficking abilities. Biomed. Pharmacother. 144, 112362. (2020 IF: 6.529; Times Cited: 32; Goodwin Laboratory Contribution: 20%.)

 

38.  **Sahrmann, P.G., *Donnan, P.H., Merz, K.M. Mansoorabadi, S.O., and Goodwin, D.C. 2020. MRP.py: A parameterizer of post-translationally modified residues. J. Chem. Inf. Model. 60, 4424-4428. (2019 IF: 4.549; Times Cited: 5)

 

37.  *Simithy, J., *Fuanta, N.R., *Alturki, M., Hobrath, J.V., Wahba, A.E., Pina, I., Rath, J., Hamann, M.T., DeRuiter, J., Goodwin, D.C., and Calderón, A.I. 2018. Slow-binding inhibition of Mycobacterium tuberculosis shikimate kinase by manzamine alkaloids. Biochemistry 52, 4923 - 4933. (2020 IF: 3.162; Times Cited: 36; Goodwin Laboratory Contribution: 40%; Simithy [Calderón lab] and Fuanta [Goodwin lab] are noted to have contributed equally to the work.)

 

36.  *Simithy, J., *Fuanta, N.R., Hobrath, J.V., Kochanowska-Karamayan, A., Hamann, M.T., Goodwin, D.C., and Calderón, A.I. 2018. Mechanism of irreversible inhibition of Mycobacterium tuberculosis shikimate kinase by ilimaquinone. Biochim. Biophys. Acta 1866, 731 – 739. (2020 IF: 3.036; Times Cited: 17; Goodwin Laboratory Contribution: 40%; Simithy [Calderón lab] and Fuanta [Goodwin lab] are noted to have contributed equally to the work.)

 

35.  *Alturki, M.S., *Fuanta, N.R., **Jarrard, M.A., Hobrath, J.V., Goodwin, D.C., *Rants’o, T.A., and Calderón, A.I. 2018. A multifaceted approach to identify non-specific enzyme inhibition: Application to Mycobacterium tuberculosis shikimate kinase. Bioorg. Medicin. Chem. Lett. 28, 802 – 808. (2020 IF: 2.823; Times Cited: 11; Goodwin Laboratory Contribution: 20%)

 

34.  *Njuma, O.J., Davis, I., *Ndontsa, E.N., *Krewall, J.R., Liu, A., and Goodwin, D.C. 2017. Mutual synergy between catalase and peroxidase activities of the bifunctional enzyme KatG is facilitated by electron-hole hopping within the enzyme. J. Biol. Chem. 292, 18408 – 18421. (2020 IF: 5.157; Times Cited: 31; Goodwin Laboratory Contribution: 75%)

 

33.  **McCarty, S.E., **Schellenberger, A., Goodwin, D.C., *Fuanta, N.R., Tekwani, B.L., and Calderón, A.I. 2015. Plasmodium falciparum thioredoxin reductase (PfTrxR) and its role as a target for antimalarial discovery. Molecules 20, 11459 – 73. (2016 IF: 4.411; Times Cited: 27; Goodwin Laboratory Contribution: 35%)

 

32.  *Huang, J., Smith, F., Panizzi, J.R., Goodwin, D.C., and Panizzi, P. 2015. Inactivation of myeloperoxidase by benzoic acid hydrazide. Arch. Biochem. Biophys. 570, 14 – 22. (2020 IF: 3.759; Times Cited: 22; Goodwin Laboratory Contribution: 10%)

 

31.  *Kudalkar, S., *Li, Y., **Muldowney, M., and Goodwin, D.C. 2015. A role for catalase-peroxidase large loop 2 revealed by deletion mutagenesis: Control of active site water and ferric enzyme reactivity. Biochemistry 54, 1648 - 1662. (2020 IF: 3.162; Times Cited: 12; Goodwin Laboratory Contribution: 100%)

 

30.  **Gordon, S., *Simithy, J., Goodwin, D.C., and Calderón, A.I. 2015. Selective Mycobacterium tuberculosis shikimate kinase inhibitors as potential antibacterials.  Perspec. Med. Chem. 7, 9 – 20. (2016 IF: 1.89; Times Cited: 40; Goodwin Laboratory Contribution: 25%)

 

29.  *Simithy, J., **Gill, G., *Wang, Y., Goodwin, D.C., and Calderón, A.I. 2015. Development of an ESI-LC-MS-based assay for kinetic evaluation of M. tuberculosis shikimate kinase activity and inhibition. Anal. Chem. 87, 2129 – 2136. (2020 IF: 6.986; Times Cited: 14; Goodwin Laboratory Contribution: 50%)

 

28.  *Njuma, O.J., *Ndontsa, E.N., and Goodwin D.C. 2014. Catalase in peroxidase clothing: Interdependent cooperation of two cofactors in the catalytic versatility of KatG. Arch. Biochem. Biophys. 544, 27 – 39. (2020 IF: 3.759; Times Cited: 55; Goodwin Laboratory Contribution: 100%)

 

27.  *Wang, Y., and Goodwin, D.C. 2013. Integral role of the I*-helix in the function of the inactive C-terminal domain of catalase-peroxidase (KatG). Biochim. Biophys. Acta 1834, 362 – 371. (2020 IF: 3.036; Times Cited: 12; Goodwin Laboratory Contribution: 100%)

 

26.  *Kudalkar, S.N., **Campbell, R.A., *Li, Y., *Varnado, C.L., **Prescott, C., and Goodwin, D.C. 2012. Enhancing peroxidatic activity of KatG by deletion mutagenesis. J. Inorg. Biochem. 116, 106 – 115. (2020 IF: 3.939; Times Cited: 18; Goodwin Laboratory Contribution: 100%)

 

25.  *Ndontsa, E.N., *Moore, R.L., and Goodwin, D.C. 2012. Stimulation of KatG catalase activity by peroxidatic electron donors. Arch. Biochem. Biophys. 525, 215 – 222. (2020 IF: 3.759; Times Cited: 27; Goodwin Laboratory Contribution: 100%)

 

24.  Tejero, J., Biswas, A., Haque, M.M., Wang, Z.Q., Hemann, C., *Varnado, C.L., Hille, R., Goodwin, D.C., and Stuehr, D.J.  2011.  Mesohaem substitution reveals how haem electronic properties can influence the kinetic and catalytic parameters of neuronal NO synthase.  Biochem. J.  433, 163 – 174. (2019 IF: 4.097; Times Cited: 12; Goodwin Laboratory Contribution: 10%)

 

23.  *Moore, R.L., *Cook, C.O., **Williams, R., and Goodwin, D.C. 2008. Substitution of strictly conserved Y111 in catalase-peroxidase:  Impact of remote interdomain contacts on active site structure and catalytic performance.  J. Inorg. Biochem. 102, 1819 – 1824. (2020 IF: 3.939; Times Cited: 5; Goodwin Laboratory Contribution: 100%)

 

22.  *Moore, R.L., **Powell, L.J., and Goodwin, D.C. 2008. The kinetic properties producing the perfunctory pH profiles of catalase-peroxidases. Biochim. Biophys. Acta. 1784, 900 – 907. (2020 IF: 3.036; Times Cited: 27; Goodwin Laboratory Contribution: 100%)

 

21.  *Baker, R.D., *Cook, C.O., and Goodwin, D.C. 2006. Catalase-peroxidase active site restructuring by a distant an inactive domain. Biochemistry 45, 7113-7121. (2020 IF: 3.162; Times Cited: 27; Goodwin Laboratory Contribution: 100%)

 

 

 

 

Resulting from research at Auburn University before tenure

 

20. *Baker, R.D., *Cook, C.O., and Goodwin, D.C. 2004. Properties of catalase-peroxidase lacking its C-terminal domain. Biochem. Biophys. Res. Comm. 320, 833-839. (2020 IF: 3.575; Times Cited: 48; Goodwin Laboratory Contribution: 100%)

 

19.  *Li, Y., and Goodwin, D.C. 2004. Vital roles of an interhelical insertion in catalase-peroxidase bifunctionality. Biochem. Biophys. Res. Comm.  318, 970-976. (2020 IF: 3.575; Times Cited: 24; Goodwin Laboratory Contribution: 100%)

 

18.  *Varnado, C.L., and Goodwin, D.C. 2004. System for the expression of recombinant hemoproteins in Escherichia coli. Prot. Exp. Purif.  35, 76-83. (2020 IF: 1.640; Times Cited: 87; Goodwin Laboratory Contribution: 100%)

 

17.  *Varnado, C.L., **Hertwig, K.M., **Thomas, R., **Roberts, J.K., and Goodwin, D.C. 2004. Properties of a novel periplasmic catalase-peroxidase from Escherichia coli O157:H7.  Arch. Biochem. Biophys. 421, 166-174. (2020 IF: 3.759; Times Cited: 48; Goodwin Laboratory Contribution: 100%)

 

16.  Goodwin, D.C., and **Hertwig, K. M. 2003.  Peroxidase-catalyzed oxidation of capsaicinoids:  Steady-state and transient-state kinetic studies.  Arch. Biochem. Biophys. 417, 18-26. (2020 IF: 3.759; Times Cited: 41; Goodwin Laboratory Contribution: 100%)

 

Publications resulting from research before coming to Auburn University

 

15.  Trostchansky, A., O-Donnell, V.B., Goodwin, D.C., Landino, L.M., Marnett, L.J., Radi, R., and Rubbo, H.  2007.  PGHS-1 in turnover is inactivated by peroxynitrite derived- radicals: Differential effect of ^.NO on peroxidase and cyclooxygenase activities. Free Rad. Biol. Med. 41, 1029 – 1038.  (2020 IF: 7.376; Times Cited: 56)

 

14.  Goodwin, D.C., Rowlinson, S.W., and Marnett, L.J.  2000.  Substitution of tyrosine for the proximal histidine ligand to the heme of prostaglandin endoperoxide synthase-2:  Implications for the mechanism of cyclooxygenase activation and catalysis. Biochemistry 39, 5422-5432. (2020 IF: 3.162; Times Cited: 24; Times Cited: 56)

 

13.  Kiefer, J.R., Pawlitz, J.L., Moreland, K.T., Stegeman, R.A., Hood, W.F., Gierse, J.K., Stevens, A.M., Goodwin, D.C., Rowlinson, S.W., Marnett, L.J., Stallings, W.C., and Kurumbail, R.G.  2000.  Structural insights into the stereochemistry of the cyclooxygenase reaction.  Nature 405, 97-101. (2019 IF: 42.778; Times Cited: 316)

 

12.  Rowlinson, S.W., Crews, B.C., Gierse, J.K., Goodwin, D.C. and Marnett, L.J. 2000.  Spatial requirements for 15-HETE synthesis within the cyclooxygenase active site of murine COX-2:  why acetylated COX-1 does not synthesize 15-R-HETE.  J. Biol. Chem. 275, 6586-6591. (2020 IF: 5.157; Times Cited: 102)

 

11.  Goodwin, D.C., Landino, L.M., and Marnett, L.J. 1999. Effects of nitric oxide and nitric oxide-derived species on prostaglandin endoperoxide synthase and prostaglandin biosynthesis.  FASEB J. 13, 1121-1136. (2019 IF: 4.966; Times Cited: 224)

 

10.  Goodwin, D.C., Landino, L.M., and Marnett, L.J. 1999. Reactions of prostaglandin endoperoxide synthase with nitric oxide and peroxynitrite. Drug Metabolism Reviews 31, 273-294. (2020 IF: 4.526; Times Cited: 30)

 

9.   Marnett, L.J., Rowlinson, S.W., Goodwin, D.C., Kalgutkar, A.S., and Lanzo, C.A.  1999. Arachidonic acid oxygenation by COX-1 and COX-2: Mechanisms of catalysis and inhibition. J. Biol. Chem. 274, 22903-22906. (2016 IF: 4.125; Times Cited: 714)

 

8.   Goodwin, D.C., Gunther, M.R., Hsi, L.C., Crews, B.C., Eling, T.E., Mason, R.P., and Marnett, L.J.  1998.  Nitric oxide trapping of tyrosyl radicals generated during prostaglandin endoperoxide synthase turnover: detection of the radical derivative of tyrosine 385. J. Biol. Chem. 273, 8903-8909. (2020 IF: 5.157; Times Cited: 166)

 

7.   Goodwin, D.C., Grover, T.A., and Aust, S.D.  1997.  Roles of efficient substrates in peroxidase-catalyzed oxidations. Biochemistry 36, 139-147. (2020 IF: 3.162; Times Cited: 58)

 

6.   Goodwin, D.C., Grover, T.A., and Aust, S.D.  1996.  Redox mediation in the peroxidase-catalyzed oxidation of aminopyrine: possible implications for drug-drug interactions. Chem. Res. Toxicol. 9, 476-483. (2020 IF: 3.739; Times Cited: 35)

 

5.   Goodwin, D. C., Aust, S. D., and Grover, T. A.  1996.  Free radicals produced during oxidation of hydrazines by hypochlorous acid.  Chem. Res. Toxicol. 9, 1333-1339. (2020 IF: 3.739; Times Cited: 30)

 

4.   Goodwin, D.C., Aust, S.D., and Grover, T.A.  1995.  Evidence for veratryl alcohol as a redox mediator in lignin peroxidase-catalyzed oxidation.  Biochemistry 34, 5060-5065. (2020 IF: 3.162; Times Cited: 113)

 

3.   Goodwin, D.C., Yamazaki, I., Aust, S.D., and Grover, T.A.  1995.  Determination of transient-state rate constants for rapid peroxidase reactions. Anal. Biochem. 231, 333-338. (2020 IF: 3.187; Times Cited: 46)

 

2.   Goodwin, D.C., Barr, D. P., Aust, S. D., and Grover, T. A.  1994.  The role of oxalate in lignin peroxidase catalyzed reduction: Protection from compound III accumulation.  Arch. Biochem. Biophys. 315: 267-272. (2020 IF: 3.759; Times Cited: 15)

 

1.   Goodwin, D.C., and Lee, S. B.  1993.  Rapid, microwave mini-prep of total genomic DNA from fungi, plants, protists and animals for PCR.  Biotechniques 15: 438- 444. (2016 IF: 1.993; Times Cited: 223)

 

4.B.b.2 Peer-Reviewed Book Chapters:

 

Resulting from research after coming to Auburn University

 

3.      *Krewall, J.R., **Minton, L.E., and Goodwin, D.C. 2020. KatG structure and mechanism: Using protein-based oxidation to confront the threats of reactive oxygen. In Bridging Structure and Function in Mechanistic Enzymology. J. M. Miller, Ed. ACS Symposium Series, 1357, 83-120. (Times Cited: 4; Goodwin Laboratory Contribution: 100%)

 

2.   Goodwin, D.C., **Laband, K.L., and **Hertwig, K.M.  2005.  Transient- and steady-state kinetics of peroxidase-catalyzed capsaicinoid oxidation.  In Phenolics in Foods and Natural Health Products. C. T. Ho and F. Shahidi, Eds.  ACS Symposium Series, 909, 161-174. (Times Cited: 0; Goodwin Laboratory Contribution: 100%)

 

Resulting from research before coming to Auburn University

 

1.   Marnett, L.J., D.C. Goodwin, S.W. Rowlinson, A.S. Kalgutkar, and L.M. Landino. 1999. Structure, function, and inhibition of prostaglandin endoperoxide synthase. In Comprehensive Natural Products Chemistry, Vol. V pp. 225-261. C.D. Poulter, Ed. Elsevier Science, Amsterdam. (Times Cited: 10)

 

4.B.b.3. Conference Proceedings:

 

Resulting from research after coming to Auburn University

 

1.   *Cook, C.O., *Moore, R.L., and Goodwin, D.C. 2008. The effect of R117 and D597 interdomain residue substitutions on the reactivation of Escherichia coli catalase-peroxidase. NOBCChE Proceedings: 35^th Annual National Conference. (Goodwin Laboratory Contribution: 100%)

 

4.B.c.   Presented Papers and Lectures

 

4.B.c.1. Invited Presentations (University Departments):

(† denotes the presenter, oral if underlined; * denotes graduate student coauthor; ** denotes undergraduate coauthor)

 

Resulting from research after coming to Auburn University

 

28.  †Goodwin, D. C. “Radicals and Switches: Synergy or Antagonism in the Operation of a Bifunctional Enzyme?” Department of Chemistry, LaGrange College, March 21, 2016.

 

27.  †Goodwin, D. C. “Tryptophanyl Radicals and Arginine Switches: Synergy or Antagonism in the Operation of a Bifunctional Enzyme?” Department of Chemistry and Biochemistry, University of North Georgia, February 5, 2016.

 

26.  †Goodwin, D. C. “Tryptophanyl Radicals and Arginine Switches: Synergy or Antagonism in the Operation of a Bifunctional Enzyme?” Department of Chemistry, Kansas State University, January 28, 2016.

 

25.  †*Njuma, O. J., Davis, I., *Ndontsa, E. N., Liu, A., and Goodwin, D.C. “Electron donors to the rescue: The proximal tryptophan as a potential conduit for catalase-peroxidase inactivation.” Department of Chemistry, University of Buea, Cameroon. April 1, 2015.

 

24.    †Goodwin, D.C. “Novel Mechanisms for Hydrogen Peroxide Degradation Catalyzed by KatG: Implications for Antibiotic Resistance and Bacterial Virulence.” Department of Chemistry and Biochemistry, Kennesaw State University, October 3, 2012. 

 

23.  †Goodwin, D. C. “The transformation of enzyme function: Commandeering an old framework for new activity.” Department of Chemistry, University of South Alabama, September 10, 2010. 

 

22. †Goodwin, D. C. “Structural requirements for the hemoprotein-dependent decomposition of hydroperoxides:  Lessons from the catalase-peroxidases.” Department of Chemistry, Georgia State University, March 20, 2009.

 

21.  †Goodwin, D. C. “Structures and Mechanisms of Hemoproteins:  Implications for Enzyme Engineering, Bacterial Virulence, and Antibiotic Resistance.” Department of Chemistry, Jacksonville State University, February 20, 2007. 

 

20.    †Goodwin, D. C. “Contribution of Protein Structural Features to the Unique Catalytic Properties of Catalase-Peroxidases:  Implications for Bacterial Virulence, Antibiotic Resistance, and Enzyme Engineering.” Department of Chemistry and Physics, Georgia College and State University, Milledgeville, GA, February 2006.

 

19.    †Goodwin, D. C. “Contribution of Protein Structural Features to the Unique Catalytic Properties of Catalase-Peroxidases:  Implications for Bacterial Virulence, Antibiotic Resistance, and Enzyme Engineering.” Department of Chemistry, University of West Florida, Pensacola, FL, October 21, 2005.

 

18.    †Goodwin, D. C. “Protein Structural Contributions to the Unique Catalytic Properties of Catalase-Peroxidases.” Department of Chemistry and Biochemistry, University of Delaware, Newark, DE, November 1, 2004.

 

17.    †Goodwin, D. C. “Protein Structural Contributions to the Unique Catalytic Properties of Catalase-Peroxidases.” Department of Biochemistry, Wake Forest University, Winston-Salem, NC, August 3, 2004. 

 

16.    †Goodwin, D. C. “Protein Structural Contributions to the Unique Catalytic Properties of Catalase-Peroxidases.” Department of Chemistry, New York University, New York, NY, April 26, 2004.

 

15.    †Goodwin, D. C. “Structural Requirements for the Hemoprotein-Dependent Decomposition of Hydroperoxides:  Lessons from the Catalase-Peroxidases.” Department of Biochemistry, Vanderbilt University, Nashville, TN, March 26, 2004.

 

14.    †Goodwin, D. C. “Hemoprotein Structure and Mechanism: Implications for Enzyme Engineering, Bacterial Virulence, and Antibiotic Resistance.” Department of Chemistry and Physics, LaGrange College, LaGrange, GA, March 10, 2004. 

 

13.    †Goodwin, D. C. “Structural Requirements for the Hemoprotein-Dependent Decomposition of Hydroperoxides:  Lessons from the Catalase-Peroxidases.” Department of Chemistry, Butler University, Indianapolis, IN, February 18, 2004.

 

12.    †Goodwin, D. C. “Structural Requirements for the Hemoprotein-Dependent Decomposition of Hydroperoxides:  Lessons from the Catalase-Peroxidases.” Department of Chemistry, Case Western Reserve University, Cleveland, OH, February 6, 2004. 

 

11.    †Goodwin, D. C. “Hemoprotein Structure and Mechanism: Implications for Enzyme Engineering, Bacterial Virulence, and Antibiotic Resistance.” Department of Chemistry and Physics, Georgia College and State University, Milledgeville, GA, February 2, 2004.

 

10.    †Goodwin D. C.  “Hemoprotein Structure and Mechanism: Implications for Enzyme Engineering, Bacterial Virulence, and Antibiotic Resistance.”  Department of Chemistry, State University of West Georgia, Carrollton, GA, April 11, 2003.

 

9.      †Goodwin, D. C.  “Hemoprotein Structure and Mechanism: Implications for Enzyme Engineering, Bacterial Virulence, and Antibiotic Resistance.” Department of Chemistry, University of Mississippi, Oxford, MS, October 18, 2002.

 

8.      †Goodwin, D. C.  “Catalase/Peroxidase Structure, Function, and Kinetics:  Implications for Antibiotic Resistance and Bacterial Virulence.”  Department of Chemistry, State University of West Georgia, Carollton, GA.  April 27, 2000.

 

7.      †Goodwin, D. C.  “Mechanisms of Prostaglandin Biosynthesis:  Generation and Trapping of Tyrosyl Radicals.” Department of Chemistry and Biochemistry, University of Texas at Arlington, Arlington, TX.  April 26, 1999.

 

6.      †Goodwin, D. C.  “Structure and Function of Catalase/Peroxidases:  Implications for Antibiotic Resistance and Virulence.” Department of Chemistry and Biochemistry, University of Texas at Arlington, Arlington, TX.  April 27, 1999.

 

Resulting from research before coming to Auburn University

 

5.   †Goodwin, D.C. “Mechanisms of Prostaglandin Biosynthesis:  Generation and Trapping of Tyrosyl Radicals.” Department of Chemistry, Auburn University, Auburn, AL.  January 29, 1999.

 

4.      †Goodwin, D.C. “Structure and Function of Catalase/Peroxidases: Implications for Antibiotic Resistance and Virulence.” Department of Chemistry, Auburn University, Auburn, AL.  April 26, 1999.

 

3.     †Goodwin, D.C. “Kinetics of redox mediation in peroxidase catalysis:  implications for metabolism of xenobiotics.”  Department of Biochemistry, Center in Molecular Toxicology, School of Medicine, Vanderbilt University, Nashville, TN.  April 2, 1996.

 

2.      †Goodwin, D.C. “Kinetics of redox mediation in peroxidase catalysis:  implications for metabolism of xenobiotics.”  Atherosclerosis, Nutrition, and Lipid Research Division, School of Medicine, Washington University, Saint Louis, MO, April 4, 1996.

 

1.      †Goodwin, D.C. “Kinetics of redox mediation in peroxidase catalysis:  implications for metabolism of xenobiotics.”  Department of Biochemistry, Michigan State University, East Lansing, MI, April 8, 1996.

 

 

4.B.c.2. Invited Presentations (Conferences):

(† denotes the presenter, oral if underlined; * denotes graduate student coauthor; ** denotes undergraduate coauthor)

 

Resulting from research after coming to Auburn University

 

6.      †Goodwin, D.C. “Radicals, switches, and a protein-based cofactor: Expanding the catalytic abilities of an old active site.” Advancements in Mechanistic Enzymology; SERMACS 2019, Savannah, GA, October 21, 2019.

 

5.      †Goodwin, D.C. “Intramolecular electron transfer for self-preservation and bifunctional catalysis.” Gordon Research Conference: Enzymes, Coenzymes, and Metabolic Pathways, Waterville Valley, NH, July 23, 2018.

 

4.      †Goodwin, D.C. “Intramolecular radical transfer: How KatG enlists self-preservation for synergistic bifunctional catalysis.” Session: Bioinorganic Chemistry in the Southeast: From Small Molecules to Macromolecules. SERMACS 2017, Charlotte, NC, November 8 2017.

 

3.   †Goodwin, D.C., *Baker, R.D., *Cook, C.O., and **Laband, K. A. “Integral Involvement of an Inactive Domain in Catalase-Peroxidase Structure and Catalysis.”  Gordon Conference: Enzymes, Coenzymes, and Metabolic Pathways, Meriden, NH, July 20, 2004.

 

2.      †Goodwin, D.C., *Baker, R.D., *Varnado, C.L., and *Li,Y. “Structural Requirements for the Hemoprotein-Dependent Decomposition of Hydroperoxides:  Lessons from the Catalase-Peroxidases.”  Symposium Title: Chemistry and Biology of Oxidative Damage.  Southeast Regional Meeting of the American Chemical Society, Atlanta, GA, November 5, 2003.

 

1.      †Goodwin, D. C., and **Hertwig, K. M. “Transient- and Steady-State Kinetics of Peroxidase-Catalyzed Capsaicinoid Oxidation.” Symposium Title: Phenolics in Foods and Natural Health Products. National Meeting of the American Chemical Society, New York, NY, September 8, 2003.

 

4.B.c.3. Presentations from submitted and accepted abstracts:

(† denotes the presenter, oral if underlined; * denotes graduate student coauthor; ** denotes undergraduate coauthor)

 

Resulting from research after coming to Auburn University

126. †*Quansah, K.N.A., and Goodwin, D.C. “Evaluation of cytochrome P450 function in the production of antibiotic secondary metabolites by a gifted Bacillus velezensis strain.” 15^th Annual Southeast Enzyme Conference, Atlanta, GA, April 26, 2025.

 

125.  †*Collins, S., *Xu, H., *Kenneson, J.R., **Minton, L.E., and Goodwin, D.C. “The Effect of pH on the Electron-donor Assisted Catalase Activity of KatG: Evaluation of Variants Targeting the Proximal Tryptophan and Arginine Switch” 75^th Southeast Regional Meeting of the American Chemical Society (SERMACS), Atlanta, GA, October 23, 2024.

 

124. †*Quansah, K.N.A., and Goodwin, D.C. “Exploiting bacterial strains as plant growth promoting rhizobacteria.” NOBCChE 51^st National Conference, Orlando, FL, October 2, 2024.

 

123.  †**Forbes, L.M., *Islam, R., and Goodwin, D.C. “Kinetic properties of Mycobacterium tuberculosis shikimate dehydrogenase.” 14^th Annual Southeast Enzyme Conference, Atlanta, GA, April 27, 2024.

 

122. †*Quansah, K.N.A., and Goodwin, D.C. “Exploiting bacterial strains as plant growth promoting rhizobacteria.” 14^th Annual Southeast Enzyme Conference, Atlanta, GA, April 27, 2024.

 

121. †*Quansah, K.N.A., and Goodwin, D.C. “Exploiting bacterial strains as plant growth promoting rhizobacteria.” NOBCChE Charter 1 Spring Conference, Hampton, VA, April 19, 2024.

 

120. †*Moen, F.S., *Olofintila, O. C., *Alam, J., Severance, B., Noel, Z. A., Goodwin, D. C., and Liles, M. R. “Capacity of diverse Bacillus species to control both oomycete and fungal pathogens.” American Society for Microbiology Microbe, Atlanta, GA, June 15, 2024.

 

119. †*Moen, F.S., *Olofintila, O. C., *Alam, J., Severance, B., Noel, Z. A., Goodwin, D. C., and Liles, M. R. “Capacity of diverse Bacillus species to control both oomycete and fungal pathogens.” Southeastern Branch American Society for Microbiology, Auburn, AL, November 4, 2023.

 

118. †*Ugochukwu, C. G., Ellis, H. R., and Goodwin, D. C. “Transcriptome and proteome analyses reveal sulfur-starvation induced Fe-replete response in Pseudomonas aeruginosa PAO1.” National Organization for the Advancement of Black Chemists and Chemical Engineers (NOBCChE), 50^th Annual National Meeting, New Orleans, LA, September 13, 2023.

 

117. †*Ugochukwu, C. G., Schwartz, T. S., Ellis, H. R., and Goodwin, D. C. “Sulfur starvation induces Fe-replete response and attenuates virulence pathways in Pseudomonas aeruginosa PAO1.” American Society for Microbiology MICROBE, Houston, TX, June 17, 2023.

 

116. †*Ugochukwu, C. G., Schwartz, T. S., Ellis, H. R., and Goodwin, D. C. “Sulfur starvation induces Fe-replete response and attenuates virulence pathways in Pseudomonas aeruginosa PAO1.” 13^th Annual Southeast Enzyme Conference, Atlanta, GA, April 22, 2023.

 

115. †*Islam, R., and Goodwin, D. C. “Shikimate pathway enzymes as candidates for multitarget inhibitor development.” 13^th Annual Southeast Enzyme Conference, Atlanta, GA, April 22, 2023.

 

114. †*Alam, M. J., Liles, M. R., McInroy, J. A., Noel, Z. A., and Goodwin, D. C. “Structural and functional insights of Bacillus cytochromes P450 that are involved in secondary metabolite biosynthesis.” 12^th Annual Southeast Enzyme Conference Atlanta, GA, April 23, 2022.

 

113. †*Aziz, T., **Mumford, R., and Goodwin, D. C. “Mechanistic insight into the initiation step of Methionine-Tyrosine-Tryptophan (MYW) Adduct in Mycobacterium tuberculosis KatG.” American Society for Biochemistry and Molecular Biology (ASBMB), Philadelphia, PA, April 4, 2022.

 

112.  †*Aziz, T. and Goodwin, D. C. “Partial Formation of a Protein-based Cofactor in M. tuberculosis KatG and Its Impact on Catalysis.” Southeast Regional Meeting of the American Chemical Society (SERMACS), Birmingham, AL, November 12, 2021.

 

111. †*Alam, M. J., Liles, M. R., McInroy, J. A., Noel, Z. A., and Goodwin, D. C. “Bacillus Secondary Metabolites as Potential Biocontrol Agents Against Plant Pathogenic Oomycetes.” Plant Health 2021 Online, American Phytopathological Society, Virtual, August 4, 2021.

 

110. †*Aziz, T. and Goodwin, D. C. “New Insight into the Protein-based Cofactor of Mycobacterium tuberculosis KatG: Toward Better Understanding an Unusual Catalase Mechanism.” Experimental Biology 2021, Virtual, April 28, 2021.

 

109. †*Alam, M. J. and Goodwin, D. C. “Properties of a CYP102A2 predicted to participate in plantazolicin biosynthesis.” 11^th Southeast Enzyme Conference, Virtual, April 10, 2021.

 

108. †**Lee, A. K., *Barton, C. M., *Krewall, J. R., **Petrus, S., and Goodwin, D. C. “Evaluating the function of tryptophans near KatG’s heme-dependent active site.” 11^th Southeast Enzyme Conference, Virtual, April 10, 2021.

 

107. †**Forbes, M., *Krewall, J. R., **Minton, L. E., and Goodwin, D. C. “An Arg switch and the formation of a protein-based cofactor in catalase-peroxidase (KatG).” 11^th Southeast Enzyme Conference, Virtual, April 10, 2021.

 

106. †*Basak, S., *Alam, M. J., McElroy, J. S., and Goodwin, D. C. “Effects of ACCase-targeting herbicides on the detection of southern crabgrass resistance using the malachite green colorimetric assay.” 11^th Southeast Enzyme Conference, Virtual, April 10, 2021.

 

105. †**Lee, A. K., **Petrus, S., *Krewall, J. R., *Barton, C. M., and Goodwin, D. C. “Impact of heme incorporation procedure on intermediates of KatG reaction with peroxides.” 52^nd Southeastern Undergraduate Research Conference, Tuscaloosa, AL, January 25, 2020.

 

104. †**Minton, L. E., *Xu, H., *Krewall, J. R., *Barton, C. M., and Goodwin, D. C. “Impact of heme incorporation procedure on intermediates of KatG reaction with peroxides.” 52^nd Southeastern Undergraduate Research Conference, Tuscaloosa, AL, January 25, 2020. (Received a poster award).

 

103. *Aziz, T., *Barton, C. M., *Krewall, J. R., *Xu, H., and †Goodwin, D. C. “Toward identification of intermediates in the formation of a novel protein-based cofactor” Gordon Research Conference: Enzymes, Coenzymes, and Metabolic Pathways, Waterville Valley, NH, July 21 - 27, 2019.

 

102. †*Krewall, J. R., **Sahrmann, P. G., and Goodwin, D. C. “Elucidating the novel features of the catalase mechanism of catalase-peroxidases” Gordon Research Conference: Enzymes, Coenzymes, and Metabolic Pathways, Waterville Valley, NH, July 21 - 27, 2019.

 

101. †**Sahrmann, P. G., *Donnan, P. H., *Krewall, J. R., and Goodwin, D. C. “Charged side chains enable KatG active site gatekeeping: A computational investigation of a peroxide-degrading enzyme.” 10^th Annual Southeast Enzyme Conference, Atlanta, GA, Atlanta, GA, April 13, 2019.

 

100. †*Aziz, T., †*Barton, C. M., and Goodwin, D. C. “Impact of heme incorporation procedure on intermediates of KatG reaction with peroxides.” 10^th Annual Southeast Enzyme Conference, Atlanta, GA, Atlanta, GA, April 13, 2019.

 

99.    †**McWhorter, K., *Xu, H., and Goodwin, D. C. “Use of multiple active-site tryptophans to direct off-catalase electron transfer and sustain the activity of a peroxide-detoxifying enzyme.” Southeast Regional Meeting of American Chemical Society (SERMACS), Augusta, GA, November 2, 2018.

 

98.    †**McWhorter, K., *Xu, H., and Goodwin, D. C. “Tryptophans in tandem: How to sustain KatG catalase activity with peroxidatic electron donors.” Herty Medal Undergraduate Research Symposium 2018, Lawrenceville, GA, September 21, 2018.

 

97.    †*Krewall, J. R., *Njuma, O. J., **Sahrmann, P., and Goodwin, D. C. “How intraprotein radical transfer and the role-reversal of heme intermediates generate a unique catalase mechanism.” 9^th Annual Southeast Enzyme Conference, Atlanta, GA, April 7, 2018.

 

96.  †*Xu, H., *Njuma, O., and Goodwin, D.C. “How an arginine switch promotes the self-preservation of an H₂O₂-degrading enzyme.” 9^th Annual Southeast Enzyme Conference, Atlanta, GA, Atlanta, GA, April 7, 2018.

 

95.    †**McWhorter, K.L., *Xu, H., and Goodwin, D.C. “Exploiting active-site tryptophans to direct off-mechanism electron transfer: Preserving the activity of peroxide-detoxifying enzymes.” 9^th Annual Southeast Enzyme Conference, Atlanta, GA, Atlanta, GA, April 7, 2018.

 

94.    †**Sahrmann, P., **McWhorter, K. L., *Krewall, J. R., and Goodwin, D. C. “Electron-hole hopping as catalytic self-preservation: How catalase-peroxidase from M. tuberculosis avoids the perils of peroxide decomposition.” 9^th Annual Southeast Enzyme Conference Atlanta, GA, Atlanta, GA, April 7, 2018.

 

93.  †*Fuanta, N. R., *Simithy, J., **Skinner, M., **Gill, G., **Childers, T., Calderón, A. I., and Goodwin D. “An approach towards rapid inhibitor screening and mechanistic evaluation of tuberculosis shikimate kinase: intrinsic and extrinsic fluorescence.” National Meeting of the National Organization for the Professional Advancement of Black Chemist and Chemical Engineers (NOBCChE), Minneapolis, MN, October 2017.

 

92.  †*Krewall, J. R., *Njuma, O. J., and Goodwin, D. C. “Role reversal between peroxidase reaction intermediates generates the distinct catalase mechanism of catalase-peroxidase.” 46^th Annual Southeast Magnetic Resonance Conference, Tallahassee, FL, October 21, 2017.

 

91.  †*Xu, H., *Krewall, J. R., *Njuma, O. J., and Goodwin, D. C. “How an arginine switch preserves the catalase activity of KatG: Strategic use of an active-site tryptophan for off-pathway electron transfer.” 46^th Annual Southeast Magnetic Resonance Conference, Tallahassee, FL, October 21, 2017.

 

90.    †*Fuanta, R., *Simithy, J., **Skinner, M., **Gill, G., **Childers, T., Calderón, A. I., and Goodwin D. “Imparting intrinsic flourescence as an approach towards rapid inhibitor screening and mechanistic evaluation of tuberculosis shikimate kinase.” 254^th National Meeting of the American Chemical Society, Washington D.C, August 2017.

 

89.    *Xu, H., *Krewall, J. R., *Njuma, O. J., Davis, I., Liu, A., and †*Goodwin, D. C. “Using an arginine switch and an active site tryptophan to direct off-pathway electron transfer: Maximizing catalase activity from a peroxidase scaffold.” Gordon Research Conference: Enzymes, Coenzymes, and Metabolic Pathways, Waterville Valley, NH, July 16 – 21, 2017.

 

88.    †*Krewall, J. R., *Xu, H., *Njuma, O. J., and Goodwin, D. C. “Directing off-pathway protein oxidation to preserve enzyme activity: At last, a role for the proximal tryptophan of KatG.” 7^th Annual Lester Andrews Symposium, Starkville, MS, May 31, 2017.

 

87.    †*Xu, H., *Krewall, J. R., *Njuma, O. J., and Goodwin, D. C. “How an arginine switch preserves the catalase activity of KatG: Strategic use of an active-site tryptophan for off-pathway electron transfer.” 7^th Annual Lester Andrews Symposium, Starkville, MS, May 31, 2017.

 

86.  †*Krewall, J. R., *Xu, H., *Njuma, O. J., and Goodwin, D. C. “Directing off-pathway protein oxidation to preserve enzyme activity: At last, a role for the proximal tryptophan of KatG.” 8^th Annual Southeast Enzyme Conference, Atlanta, GA, April 8, 2017.

 

85.  †*Xu, H., *Krewall, J. R., *Njuma, O. J., and Goodwin, D. C. “How an arginine switch preserves the catalase activity of KatG: Strategic use of an active-site tryptophan for off-pathway electron transfer.” 8^th Annual Southeast Enzyme Conference, Atlanta, GA, April 8, 2017.

 

84.    †*Fuanta, N. R., *Simithy, J., **Gill, G., **Kollhoff, A., **Childers, T., Calderón, A. I., and Goodwin D. “Towards high-throughput drug screening and mechanistic evaluation of tuberculosis shikimate kinase; Intrinsic protein fluorescence.” National Organization for the Professional Advancement of Black Chemist and Chemical Engineers (NOBCChE), Raleigh, NC, November 2016.

 

83.    †*Njuma, O. J., Davis, I., *Ndontsa, E. N., Liu, A., and Goodwin, D.C. “Pathways and regulation of intramolecular electron transfer in catalase-peroxidases (KatG).” BEST Symposium, DOW Chemical Company, October 1, 2016.

 

82.  †*Fuanta, N. R., *Simithy, J., **Gill, G., **Kollhoff, A., **Childers, T., Calderón, A. I., and Goodwin D. C. “Targeted intrinsic protein fluorescence, an approach towards high-throughput drug screening and mechanistic evaluation of tuberculosis  shikimate kinase.” Southeast Regional Meeting of American Chemical Society (SERMACS), Columbia, SC, October 2016.

 

 

81.  †*Alturki, M. S., **Jarrard, M. A., *Fuanta, N. R., Goodwin, D. C., and Calderón, A. I. “LC-MS based approach to characterize non-specific binding inhibitors to Mycobacterium tuberculosis shikimate kinase (MtSK).” 64^th American Society for Mass Spectrometry National Conference on Mass Spectrometry and Allied Topics, San Antonio, TX. June 5, 2016.

 

80.  †Calderón, A. I., *Simithy, J., Goodwin, D. C., and Hamann, M. T. “Mass spectrometry based studies on irreversible inhibition of recombinant Mycobacterium tuberculosis shikimate kinase by the marine sponge metabolite ilimaquinone. 64^th American Society for Mass Spectrometry National Conference on Mass Spectrometry and Allied Topics, San Antonio, TX, June 5, 2016.

 

79.  †*Njuma, O. J., Davis, I., *Ndontsa, E. N., Liu, A., and Goodwin, D.C. “The proximal tryptophan as a potential conduit for catalase-peroxidase inactivation. 42^nd National Organization for the Professional Advancement of Black Chemists and Chemical Engineers (NOBCCHE), Orlando, FL, September 21, 2015.

 

78.  †*Njuma, O. J., Davis, I., *Ndontsa, E. N., Liu, A., and *Goodwin, D. C. “Proximal tryptophan and arginine switch participation in catalase-peroxidase inactivation.” Gordon Research Conference: Enzymes, Coenzymes, and Metabolic Pathways, Waterville Valley, NH, July 13 – 14, 2015.

 

77.  †*Njuma, O. J., Davis, I., *Ndontsa, E. N., Liu, A., and Goodwin, D. C. 2015. Participation of the proximal tryptophan as a potential conduit for catalase-peroxidase inactivation. 6^th Annual Southeast Enzymes Conference, Georgia State University, Atlanta, GA, April 11, 2015.

 

76.    †*Fuanta, R., *Simithy, J., **Gill, G., **Kollhoff, A., **Childers, T., Calderón, A. I., and    Goodwin D. C. 2015. Site-directed incorporation of intrinsic fluorescence in shikimate kinase to evaluate catalysis and inhibition. 6^th Annual Southeast Enzymes Conference, Georgia State University, Atlanta, GA, April 11, 2015.

 

75.   †*Njuma, O. J., *Ndontsa, E. D., and Goodwin, D. C. “Evaluating the role of peroxidatic reducing substrates in an unusual catalase activity of catalase-peroxidases.” 2014 Symposium, The Protein Society, San Diego, CA, July 27, 2014.

 

74.  †*Simithy, J., Goodwin, D., Hamann, M.T., and Calderón, A.I. “Evaluation of the inhibitory activity of marine natural compounds against Mycobacterium tuberculosis shikimate kinase (MtSK) by LC-MS.” 62^nd American Society for Mass Spectrometry Conference on Mass Spectrometry and Allied Topics, Baltimore, MD, June 18, 2014.

 

73.  †*Njuma, O. J., *Ndontsa, E. D., and Goodwin, D. C. “Synergistic effect of peroxidatic electron donors on the catalase activity of catalase-peroxidase.” 5^th Annual Southeast Enzymes Conference, Georgia State University, Atlanta, GA, April 4, 2014.

 

72.  †*Njuma, O. J., *Ndontsa, E. N. and Goodwin, D. C. “Evaluating the role of electron donors in a novel mechanism of H₂O₂ decomposition by catalase-peroxidase.” 91^st  Alabama Academy of Science Meeting (AAS), Auburn University, AL, March 13, 2014. (Awarded 1^st Place Presentation for Chemistry Section).

 

71.  †**McCurdy, E., *Ndontsa, E. N., and Goodwin, D. C. “W438 and the diminished necessity for peroxidatic rescue of KatG catalatic turnover.”  34^th Annual Undergraduate Research Conference, University of Memphis, Memphis, TN, February 22, 2014.

 

70.  †**McCurdy, E., *Ndontsa, E. N., and Goodwin, D. C. “An investigation of W438 as a potential route for off-Pathway electron transfer and its relationship to the bifunctional activity of catalase-peroxidase.”  Southeast Regional Meeting of the American Chemical Society (SERMACS), Atlanta, GA, November 13, 2013.

         (Awarded first prize for undergraduate poster session)

 

69.  †*Njuma, O. J., *Ndontsa, E. N., and Goodwin, D. C. “Rescue of catalase-inactive intermediates of KatG by peroxidatic electron donors.” Southeast Regional Meeting of the American Chemical Society (SERMACS), Atlanta, GA, November 13, 2013.

 

68.  †*Njuma, O. J., *Ndontsa, E. N and Goodwin, D.C. “KatG: Improvisation of novel peroxide decomposition mechanisms. 99th Annual Southeastern Branch of the American Society of Microbiology Meeting (SEBASM), Auburn University, AL, November 8, 2013.

 

67.  †*Duan, H., Suh, S.-J., and Goodwin, D. C. “Mechanism for stimulation of bacterial defenses against H₂O₂ by peroxidatic electron donors.”  99th Annual Southeastern Branch of American Society of Microbiology Meeting (SEBASM), Auburn University, AL, November 8, 2013.

 

66.  †*Njuma, O. J., *Ndontsa, E. N., and Goodwin, D. C. “Electron donors to the rescue: Evaluating a novel mechanism of hydrogen peroxide decomposition by catalase-peroxidases.” National Meeting of the National Organization for the Professional Advancement of Black Chemists and Chemical Engineers (NOBCChE), Indianapolis, IN, October 3, 2013.

 

65.  †*Njuma, O. J., *Ndontsa, E. N., and Goodwin, D. C. “Surprising role of peroxidatic electron donors in the catalase activity of catalase-peroxidase.” Diversity Awareness Symposium, Department of Chemistry, University of Alabama, Tuscaloosa, AL, April 27, 2013. (Award-winning poster)

 

64.    †*Ndontsa, E. N., and Goodwin D. C. “Multiple mechanisms for KatG catalase activity: Electron donors, pH, and an arginine ‘switch.’” 2012 Annual Meeting of the Southeast Region of the American Chemical Society (SERMACS), Raleigh, NC, November 14 – 17, 2012.

 

63.    †*Ndontsa, E. N., and Goodwin, D. C. “Role of Arg 418 switch in electron-donor-enhanced catalase activity of M. tuberculosis catalase-peroxidase (KatG).” 39^th Annual National Conference NOBCChE, Washington, D.C., September 24 – 28, 2012.

 

62.    †*Ndontsa, E. N., and Goodwin, D. C. “Role of Arg 418 switch in electron-donor-enhanced catalase activity of M. tuberculosis catalase-peroxidase (KatG).” Third Southeast Enzymes Conference, Atlanta, GA,

 

61.  †*Wang, Y., and Goodwin, D. C. “The participation of conserved I’-helix in structure, stability, and catalytic function of KatG.” Third Southeast Enzymes Conference, Atlanta, GA, April 14, 2012.

 

60.  †*Duan, H., and Goodwin, D. “Essential role of distant interdomain interactions in H₂O₂ decomposition by catalase-peroxidases.”  18^th Annual Meeting of the Society for Free Radical Biology and Medicine, Atlanta, GA, November 16 – 22, 2011.

 

59.  *Wang, Y., and Goodwin, D. “Contribution of an ‘inactive’ domain to rapid H₂O₂ decomposition by KatG.” 18^th Annual Meeting of the Society for Free Radical Biology and Medicine, Atlanta, GA, November 16 – 22, 2011.

 

58.  †*Ndontsa, E. N., and Goodwin, D. C. “An improvised mechanism for H₂O₂ disproportionation based on an old enzyme scaffold.” 18^th Annual Meeting of the Society for Free Radical Biology and Medicine, Atlanta, GA, November 16 – 22, 2011.

 

57.  †*Ndontsa, E. N., and Goodwin, D. C. “An improvised mechanism for H₂O₂ disproportionation based on an old enzyme scaffold. Southeast/Southwest Regional Meeting, National Organization for the Professional Advancement of Black Chemists and Chemical Engineers (NOBCChE), Auburn, AL, November 11 – 12, 2011. (1^st Place award winning presentation)

 

56.  †*Kudalkar, S. N., and Goodwin, D. C. “Tracing the Impact of a Unique Loop in Catalase-peroxidase Catalysis.” Annual Meeting of the American Society for Biochemistry and Molecular Biology, Washington, D. C., April 9 – 13, 2011.

 

55.  †*Kudalkar, S. N., and Goodwin, D. C. “Dependence of catalytic ability of catalase-peroxidase on intersubunit interactions.” Annual Meeting of the American Society for Biochemistry and Molecular Biology, Washington, D. C., April 9 – 13, 2011.

 

54.  †*Kudalkar, S. N., and Goodwin, D. C., “ Effects of progressive deletion of a unique loop on structure and function of catalase-peroxidases.” Second Southeast Enzymes Conference, Atlanta, GA, April 2, 2011.

 

53.  †*Wang, Y., and Goodwin, D. C. “Borrowing the E. coli catalase-peroxidase C-terminal domain as a scaffold for generation of new heme-dependent catalysts.”  Second Southeast Enzymes Conference, Atlanta, GA, April 2, 2011.

 

52.  †*Ndontsa, E., and Goodwin, D. C. “Stimulation of catalase activity of catalase-peroxidases by peroxidase reducing substrates: New functions from old scaffolds.” Second Southeast Enzymes Conference, Atlanta, GA, April 2, 2011.

 

51.  †*Goodwin, D. C., *Ndontsa, E. N., and *Moore, R. “A new role for the vestigial peroxidase function of KatG:  pH-dependent catalase activation.” Gordon Conference: Enzymes, Coenzymes, and Metabolic Pathways, Waterville Valley, NH, July 18 – 23, 2010.

 

50.  †*Kudalkar, S. N., and Goodwin, D. C. “Impact of intersubunit interactions on catalytic versatility of catalase-peroxidases.” First Southeast Enzyme Conference, Atlanta, GA, April 10, 2010.

 

49.  †*Goodwin, D.C.,*Li, Y, *Kudalkar, S., **Campbell, R., and **Prescott, C. “Roles of insertional sequences in commandeering an existing enzyme framework for new catalytic function:  A case study in catalase-peroxidases.” Gordon Conference: Enzymes, Coenzymes, and Metabolic Pathways, Waterville Valley, NH, July 5 – 10, 2009.

 

48.  †*Moore, R. M., and Goodwin, D. C. “ Activation of oxygen production by reducing substrates in E. coli catalase-peroxidase.” Gordon Conference: Metals in Biology, Ventura, CA, January 25 – 30, 2009.

 

47.  †*Cook, C.O., *Moore, R.L., and Goodwin, D. C. “Role of R117 and D597 interdomain residues in the reactivation of E. coli catalase-peroxidase.” American Chemical Society, 235th National Meeting, New Orleans, LA, April 6 – 10, 2008.

 

46.  †*Cook, C.O., and Goodwin, D.C. “Role of the central hydrogen bonding network interdomain residues in the bifunctionality of catalase-peroxidases.” NOBCChE 35th Annual Conference, Philadelphia, PA, March 17, 2008.

 

45.  †*Cook, C.O., *Moore, R.L., Goodwin, D.C. “Effect of distant, intradomain residues on restoring the catalase-peroxidase bifunctional active site.” Southeast Regional Meeting of the American Chemical Society, Greenville, SC, October 14 – 27, 2007.

 

44.  †*Moore, R.L., **Williams, R., and Goodwin, D.C. “Role of interdomain interaction of tyrosine 111 on catalase-peroxidase.” Southeast Regional Meeting of the American Chemical Society, Greenville, SC, October 14 – 27, 2007.

 

43.  †Whitley, E.M., Goodwin, D.C., Cupp, M.S., Todd, L.W., Zhang, D., Mount, J.D., **Powell, L.J., and Cupp, E.W. 2007. “Conformational and functional stability and immunogenicity of a vasoactive insect salivary protein.” Experimental Biology Annual Meeting, Washington, DC.

 

42.  †*Varnado, C.L., Olson, J.S., and Goodwin D.C. “Expression of recombinant hemoproteins in E. coli using a heme protein expression system.” 51^st Annual Meeting of the Biophysical Society, Baltimore, MD, March 3 – 7, 2007.

 

41.  †*Goodwin, D.C., *Cook, C.O., *Moore, R.L. “Roles of distant but highly conserved interactions in maintaining active site function in catalase-peroxidases.” Gordon Conference: Enzymes, Coenzymes, and Metabolic Pathways, Biddeford, ME, July 8 – 13, 2007.

 

40.  †*Cook, C. O., *Moore, R. L., Goodwin, D. C. “Role of intrasubunit interactions between domains in catalase-peroxidase structure and activity.” American Chemical Society, 233^rd National Meeting, Boston, MA, August 19 – 23, 2007.

 

39.  †*Goodwin, D. C., *Cook, C. O., *Baker, R. D. “Modulation of catalase-peroxidase active site structure and catalysis by distant protein structures.” American Chemical Society, 231^st National Meeting, Atlanta, GA, March 26 – 30, 2006.

 

38.  †*Moore, R., Goodwin, D. C., ^§Laband, K. A., and ^†Powell, L. “Role of interdomain salt bridge on catalase-peroxidase activity.” American Chemical Society, 231^st National Meeting, Atlanta, GA, March 26 – 30, 2006.

 

37.  †*Cook, C. O., *Baker, R., and Goodwin, D. C. “Function of a gene-duplicated domain in catalase-peroxidase structure and activity.” American Chemical Society, 231^st National Meeting, Atlanta, GA, March 26 – 30, 2006.

 

36.  †*Li, Y., and Goodwin D. C. “Central participation of an interhelical insertion in catalase-peroxidase bifunctionality and resistance to peroxide-dependent inactivation.” Southeast Regional Meeting of the American Chemical Society, Research Triangle Park, NC, November 11, 2004.

 

35.  †*Baker, R. D., *Cook, C. O., and Goodwin D. C. “Essential contribution of the C-terminal domain to the structure of the catalase-peroxidase active site.”  Southeast Regional Meeting of the American Chemical Society, Research Triangle Park, NC, November 11, 2004.

 

34.  †*Cook, C. O., *Baker, R. D., and Goodwin, D. C. “Catalase-peroxidase active site restructuring by a distant and inactive domain.” Southeast Regional Meeting of the American Chemical Society, Research Triangle Park, NC, November 11, 2004.

 

33.  †**Laband, K. A., *Baker, R. D., and Goodwin, D. C. “Contributions of an interdomain ion pair to the bifunctional properties of catalase-peroxidases.”  Southeast Regional Meeting of the American Chemical Society, Research Triangle Park, NC, November 13, 2004. (2^nd Place Award Undergraduate Talk, Inorganic Division).

 

32.  *Varnado, C. L., and Goodwin D. C. Heme- and peroxide-dependent formation of a novel crosslink in catalase-peroxidases.  Southeast Regional Meeting of the American Chemical Society, Research Triangle Park, NC, November 10, 2004.

 

31.  *Varnado, C. L., and Goodwin, D. C. “Characterization of a novel periplasmic catalase-peroxidase. Southeast Regional Meeting of the American Chemical Society, Atlanta, GA., November 17, 2003.

 

30.  †*Baker, R., and Goodwin D. C. Insight into the Role of the C-Terminal Domain in Catalase-Peroxidase Function. Southeast Regional Meeting of the American Chemical Society, Atlanta, GA, November 17, 2003.

 

29.  †**Laband, K. A., and Goodwin D. C. “Peroxidase-catalyzed oxidation of plant-derived o-methoxyphenols: Implications for the metabolism of health-promoting phenolic compounds.” Southeast Regional Meeting of the American Chemical Society, Atlanta, GA, November 18, 2003. (1^st Place Award Undergraduate Poster)

 

28.  †*Li, Y., and Goodwin D. C. “Use of deletion mutagenesis to determine the novel functions of two unique interhelical insertions in catalase-peroxidases. Southeast Regional Meeting of the American Chemical Society, Atlanta, GA, November 18, 2003.

 

27.  †Goodwin, D. C., *Baker, R., and *Li, Y. “Protein Structural Contributions to the Unique Catalytic Properties of Catalase-Peroxidases. American Chemical Society, 226^th National Meeting, New York, NY. September 7, 2003.

 

26.  †*Baker, R., and Goodwin, D. C. “Essential role of the C-terminal domain in catalase-peroxidase function.”  American Chemical Society, 226^th National Meeting, New York, NY, September 9, 2003.

25. †*Li, Y., and Goodwin, D. C. “Roles of two interhelical insertions in catalase-peroxidase bifunctionality.”  American Chemical Society, 226^th National Meeting, New York, NY, September 9, 2003.

 

24.  †*Varnado, C. L., **Hertwig, K. M., **Thomas, R., **Roberts, J. K., and Goodwin, D. C. 2003. “Spectral and kinetic properties of a novel periplasmic catalase-peroxidase.”  American Chemical Society, 226^th National Meeting, New York, NY, September 10, 2003.

 

23.  †*Goodwin, D. C., *Baker, R., *Varnado, C. L., and *Li, Y. “Protein structural contributions to the unique catalytic properties of catalase-peroxidases. Gordon Conference: Enzymes, Coenzymes, and Metabolic Pathways, Meriden, NH, July 14-17, 2003.

 

22.  †*Varnado, C. L., and Goodwin, D. C. “Design of a specialized expression system for recombinant hemoproteins.” Southeast Regional Meeting of the American Chemical Society, Charleston, South Carolina, November 14, 2002.

 

21.  †*Baker, R., *Li, Y., and Goodwin D. 2002. Selective elimination of catalase activity from catalase-peroxidase by deletion mutagenesis. Southeast Regional Meeting of the American Chemical Society, Charleston, South Carolina, November 15, 2002.

 

20.  †Goodwin, D. C., *Li, Y., and *Baker, R. Selective elimination of catalase activity from catalase-peroxidase by deletion mutagenesis. Gordon Conference: Enzymes, Coenzymes, and Metabolic Pathways, Meriden, NH, July 23 - 24, 2002.

 

19.  †**Hertwig, K. M., and Goodwin, D. C. “Characterization of a novel, extracellular catalase-peroxidase from E. coli O157:H7.” Council on Undergraduate Research, Posters on the Hill Forum, Washington, D.C. April 18, 2002.

 

18.  †**Hertwig, K. M. and Goodwin, D. C.  “Cloning, overexpression, purification, and characterization of catalase/peroxidase from enterohemorrhagic E. coli O157:H7.” Amer. Chem. Soc. Southeast Regional Meeting, Savannah, GA, September 25, 2001

 

17.    †*Li, Y., Melius, P., and Goodwin, D. C. “Activation of bacterial catalase-peroxidases by addition of hemin.” Amer. Chem. Soc., Southeast Regional Meeting, Savannah, GA, September 24, 2001.

 

16.  †*Hertwig, K. and Goodwin, D. C. Cloning, overexpression, purification, and characterization of catalase/peroxidase from enterohemorrhagic E. coli O157:H7. Amer. Chem. Soc. 222nd National Meeting, Chicago, IL, August 28, 2001.

 

Resulting from research before coming to Auburn University

 

15.  †Goodwin, D.C., Rowlinson, S. W., and Marnett, L. J. 1998.  Heme oxidation states in prostaglandin endoperoxide H synthase catalytic mechanism. Amer. Chem. Soc. 216th National Meeting, Boston, MA.

 

14.  †Rowlinson, S.W., Crews, B. C., Goodwin D. C., and Marnett L. J. 1998. Structure/function analysis on the cyclooxygenase channel of mouse prostaglandin endoperoxide synthase-2. Amer. Chem. Soc. 216th National Meeting, Boston, MA.

 

13.  †Goodwin, D.C., Gunther, M. R., Hsi, L. C., Crews, B. C., Eling, T. E., Mason, R. P., and Marnett, L. J. 1997. Nitric oxide trapping of the Y385 radical during prostaglandin endoperoxide synthase turnover. Intl. Congress Biochemistry Mol. Biol./Amer. Soc. Biochemistry Mol. Biol. Joint Meeting, San Francisco, CA.

 

12.  †Goodwin, D.C., Aust, S. D., and Grover, T. A.  1996.  Enhancement of peroxidase-catalyzed oxidation of hydrazine derivatives by chlorpromazine. Amer. Soc. Biochemistry Mol. Biol. National Meeting, New Orleans, LA.

 

11.  †Goodwin, D.C., Aust, S. D., and Grover, T. A.  1996.  Enhancement of peroxidase-catalyzed xenobiotic oxidation by phenothiazines. Soc. Toxicol. Annual Meeting, Anahiem, CA.

 

10.  †Goodwin, D.C., Aust, S. D., and Grover, T. A.  1995.  Phenothiazines as redox mediators in peroxidase-catalyzed xenobiotic oxidation. Soc. Toxicol. Mountain West Chapter Annual Meeting, Ft. Collins, CO.

 

9.      †Goodwin, D. C., Yamazaki, I., Aust, S. D., and Grover, T. A.  1995.  Determination of transient-state rate constants for peroxidase reactions. Amer. Soc. Biochemistry Mol. Biol./Amer. Chem. Soc. Div. Biol. Chem. National Meeting, San Francisco, CA.

 

8.   †Goodwin, D.C., Aust, S. D., and Grover, T. A.  1995.  Redox mediators in lignin peroxidase catalysis: A kinetic model. Amer. Soc. Biochemistry Mol. Biol./Amer. Chem. Soc. Div. Biol. Chem. National Meeting, San Francisco, CA.

 

7.   †Grover, T.A., Goodwin, D. C., Barr, D. P., and S.D. Aust.  1994.  Protection of lignin peroxidase activity: oxalate and cation radicals. Intl. Soc. Free Rad. Res. 7th Biennial Meeting, Sydney, Australia.

 

6.   †Goodwin, D.C., Aust, S. D., and Grover, T. A. 1994. Veratryl alcohol (VA) mediated oxidation by lignin peroxidase. Intl. Soc. Free Rad. Res. 7th Biennial Meeting, Sydney, Australia.

 

5.   †Goodwin, D.C., Barr, D. P., Aust, S. D., and Grover, T. A. 1994. Inactivation of lignin peroxidase of Phanerochaete chrysosporium by oxygen radicals. Amer. Soc. for Microbiol. 94th General Meeting, Las Vegas, NV.

 

4.      †Goodwin, D. C., Barr, D. P., Aust, S. D., and Grover, T. A. 1994. The novel role of the fungal metabolite oxalate in the catalytic cycle of lignin peroxidase. Amer. Soc. Microbiol. Intermountain Branch Annual Meeting, Provo, UT.

 

3.   †Johnston, C.G., Goodwin, D. C., and Aust, S. D. 1994. Use of ribosomal DNA for species delineation and detection of Phanerochaete spp. Amer. Soc. Microbiol. 94th General Meeting, Las Vegas, NV.

 

2.      †Goodwin, D. C., Johnston, C. G., Aust, S. D., and Grover, T. A. 1993. Microwave extraction of DNA from fungi in soil: a simple, rapid method for polymerase chain reaction. Amer. Soc. Microbiol., 93rd General Meeting, Atlanta, GA.

 

1.         †Goodwin, D.C., and Lee, S. B. 1992. Ribosomal DNA sequences of Leptomitus lacteus, Sapromyces elongatus, Aquilinderella fermentans, and Rhipidium sp. and  their evolutionary implications for the Oomycete order Leptomitales. Soc. Study Evol., University of California, Berkeley, CA.

 

4.B.c.4. Auburn University Publications and Presentations:

(† denotes the presenter, oral if underlined; * denotes graduate student coauthor; ** denotes undergraduate coauthor)

 

23.  †*Moen, F.S., *Olofintila, O. C., *Alam, J., Severance, B., Noel, Z. A., Goodwin, D. C., and Liles, M. R. “Capacity of diverse Bacillus species to control both oomycete and fungal pathogens.” Auburn University Research Symposium, March, 2024.

 

22.    †**Warner, D., *Alam, M. J., *Moen, F., Noel, Z., Goodwin, D. C., and Liles, M. “Identifcation of Bacillus strains that inhibit plant fungal and/or oomycete pathogens.” 2020 Auburn Research: Virtual Student Symposium, March 2021.

 

21.  †**Forbes, M. G., **Minton, L. E., *Krewall, J. R., and Goodwin, D. C. “Identifying heme intermediates of protein-based cofactor formation in catalase-peroxidase (KatG).” 2020 COSAM Undergraduate Research Fair, November 2020.

 

20.   †**Minton, L. E., *Krewall, J. R., *Xu, H., and Goodwin, D. C. “The effect of a pH-dependent arginine switch on protein-based cofactor formation in catalase-peroxidase (KatG).” 2020 Auburn Research: Virtual Student Symposium, April 2020. (UG Poster Award Winner for COSAM)

 

19.  †**Sahrman, P., **McWhorter, K., *Krewall, J. R., and Goodwin, D.C. 2018. “Electron-hole hopping as catalytic self-preservation: How catalase-peroxidase from Mycobacterium tubercu­losis avoids the perils of peroxide decomposition.” Auburn U. J. Undergrad. Scholarship (AUJUS) 7, 47 – 48.

 

18.    †**McWhorter, K. “Exploiting active-site tryptophans for off-pathway electron transfer: Preserving the activity of peroxide detoxifying enzymes.” This is Research Student Symposium, March 26, 2018.

 

17.    †**Sahrmann, P. “Electron-hole hopping as catalytic self-preservation: How catalase-peroxidase from M. tuberculosis avoids the perils of peroxide decomposition.” This is Research, Student Symposium, March 26, 2018.

 

16.    †*Njuma, O.J. “Radical Mechanisms for Catalase-Peroxidase (KatG) activity, inactivation, and restoration” This is Research, Student Symposium, April 13, 2016.   

 

15.    †**Snider, O.H. “Kanamycin oxidation by KatG: A new mechanism for aminoglycoside anitibiotic resistance?” AU Cellular and Molecular Biosciences: Undergraduate Summer Research Scholars Colloquium, July 24, 2015.

 

14.    **McCurdy, E., **Barr, L.E., *Njuma, O.J., *Ndontsa, E.N., and Goodwin, D.C. 2015. Evaluating the novel role of Trp 438 in active turnover of M. tuberculosis catalase-peroxidase. Auburn U. J. Undergrad. Scholarship (AUJUS) 4, 27 – 32.

 

13.    †**Kollhoff, A., and Goodwin, D.C. “Production of a tuberculosis shikimate kinase variant for inhibitor analysis by mechanistically targeted intrinsic protein fluorescence” This is Research, Student Symposium, April 13, 2015.

 

12.    †*Njuma, O.J. “Potential participation of the proximal tryptophan and arginine switch in catalase-peroxidase inactivation.” This is Research, Student Symposium, April 13, 2015.

 

11.    †**Barr, L.E, **McCurdy, E., *Njuma, O., and Goodwin, D.C. “Evaluating potential routes of off-pathway electron transfer in catalase-peroxidases.” This is Research, Student Symposium, April 13, 2015.

 

10.    †*Fuanta, N.R. “Site-directed incorporation of intrinsic fluorescence in shikimate kinase to evaluate catalysis and inhibition.” This is Research, Student Symposium, April 13, 2015.

 

9.   †**Kollhoff, A., and Goodwin, D.C. “Production of a tuberculosis shikimate kinase variant for inhibitor analysis by mechanistically targeted intrinsic protein fluorescence” AU Cellular and Molecular Biosciences: Undergraduate Summer Research Scholars Colloquium, July 25, 2014.

 

8.      †**Gill, G., and Goodwin, D.C. “Isolation and kinetic characterization of Mycobacterium tuberculosis shikimate kinase.” AU Cellular and Molecular Biosciences: Undergraduate Summer Research Scholars Colloquium, July 26, 2013.

 

7.      †Goodwin, D.C. “Novel mechanisms for hydrogen peroxide degradation catalyzed by KatG: Implications for antibiotic resistance and bacterial virulence.” Pharmacal Sciences Graduate Seminar, April 10, 2012.

 

6.      †**Suh, Jordan, and Goodwin, D.C. “Using cysteine substitutions to investigate unique structural features of KatG.” AU Cellular and Molecular Biosciences: Undergraduate Summer Research Scholars Colloquium, July 26, 2011.

 

5.      †**Ransom, S. “The integral roles of peripheral protein structures in the function of KatG from Mycobacterium tuberculosis.” AU Cellular and Molecular Biosciences: Undergraduate Summer Research Scholars Colloquium, July 28, 2010.

 

4.      †Goodwin, D.C. “A tale of two domains: How long-distance relationships modulate enzyme function.” Special Topics in Kinesiology, B. Gladden (faculty organizer), School of Kinesiology, October 1, 2009.

 

3.      †**Campbell, R. “Contribution of an interhelical insertion to catalase-peroxidase bifunctionality and resistance to peroxide-dependent inactivation.” AU Undergraduate Research Forum, March 13, 2009.

 

2.      †**Campbell, R. “Contribution of an interhelical insertion to catalase-peroxidase bifunctionality and resistance to peroxide-dependent inactivation. AU Cellular and Molecular Biosciences: Undergraduate Summer Research Scholars Colloquium, August 8, 2008.

 

 

1.      †**Hertwig, K. “Cloning, overexpression, purification, and characterization of catalase/peroxidase from enterohemorrhagic E. coli O157:H7.” Auburn University Graduate Research Forum, Auburn, AL. 2001.

 

4.B.f.   Patents and Inventions

 

3.      Hong, J. W., Goodwin, D., Duin, E. C., Jambovane, S., *Moore, R., Nam, T.-J., and Kim, S.-K. Systems for and methods of characterizing reactions. U.S. Patent Application # 2010/0311,611.

 

2.      *Varnado, C., Olson, J. S., and Goodwin, D. C. Increasing recombinant Hemoglobin expression for blood substitute production in E. coli by Co-Expression with the heme receptor gene (chuA) from E. coli 0157:H7. Invention Disclosure Filed with Rice University.

 

1.      Goodwin, D. C., and *Varnado, C. System for the Expression of Recombinant Hemoproteins in Escherichia coli. U.S. Provisional Patent # 60/375,347

 

 

4.B.g. Grants and Contracts

 

4.B.g.1. Extramural Sources

 

Pending Funding:

 

Current Funding:

 

BASF: Seed Treatment – Biologicals; Global R&D, Agricultural Solutions

PI: Liles, M.

Co-PI: Goodwin, D. C.

Title: Bacillus and Paenibacillus PGPR strains: genomics to metabolites

Amount: $175,000

 

United States Department of Agriculture (STTR USDA 2402286)

            PI: Mead, D. (Terra BioForge, Inc.)

            Co-PIs: Noel, Z. A., Liles, M. R., and Goodwin D. C.

Title: STTR Phase I: Synthetic biology solutions for microbial crop protection against fungal and oomycete pathogens

            Amount: $275,000

 

Previously Funded:

 

National Science Foundation (MCB-1616059)

PI: Goodwin, D. C.

Dates: 8/1/16 – 7/31/21

Title: Conduits and Control of KatG Intramolecular Electron Transfer: Formation and Operation of a Novel Cofactor

Amount: $569,549

 

 

National Institutes of Health (2R01DK093810-04)

PI: Easley, C.J.

Co-PI: Judd, R.; Co-I: Goodwin, D.C.

Dates: 02/17/16 – 02/28/17

Title: Mouse-on-a-chip systems to evaluate pancreas-adipose tissue dynamics in vitro

Amount: $1,463,980

Contribution: 5%; my role on this project is related to my background in nutritional biochemistry.

 

National Science Foundation (MCB-0641614)

PI:  Goodwin, D. C.

Dates:  7/1/07 – 6/30/12

Title: Indispensable roles of an inactive domain in catalase-peroxidase catalysis: Applications for enzyme engineering

Amount: $434,182

 

National Science Foundation (MCB-0641614 - supplement)

PI:  Goodwin, D. C.

Dates:  7/1/09 – 6/30/10

Title: Indispensable roles of an inactive domain in catalase-peroxidase catalysis:  Applications for enzyme engineering (Supplement)

Amount: $25,353 (for upgrade of Applied Photophysics Stopped-Flow spectrometer)

 

USDA, Hatch Grant and Alabama Agricultural Expt Station Special Grants Program  PD: Whitley, E. 

Co-PDs: Wolfe, D., Edmonson, M., Goodwin, D.C.

Dates: 6/01/07 – 5/31/08

Title: Development of Vaccines Targeting Horn Flies

Amount: $185,000

Contribution: 5%; a minimum of summer salary support; one laboratory undergraduate contributed to the project

 

USDA CSREES (2006-34528-17542)

PD: Wolfe, D. F.

Co-PD’s: Whitley, E., Abrams, M., Zhang, D., Goodwin, D. C.

Dates: 05/15/06 – 05/14/07

Title: Immunization of cattle against horn fly blood feeding

Amount: $185,000

Contribution: 5%; a minimum of summer salary support; one laboratory undergraduate contributed to the project

 

Petroleum Research Fund, American Chemical Society (38802 – G4)

PI: Goodwin, D. C.

Dates: 01/01/03 – 09/31/05

Title: Understanding the bifunctional active site of catalase-peroxidases: Insights for enzyme engineering.

Amount: $35,000. 

 

Not funded:

 

National Science Foundation (STTR NSF 2208111)

            PI: Mead, D. (Terra Bioworks, Inc.)

            Co-PIs: Noel, Z. A., Liles, M. R., and Goodwin D. C.

Title: STTR Phase I: Synthetic biology solutions for microbial crop protection against fungal and oomycete pathogens

            Amount: $257,117

 

National Science Foundation

PI: Ellis, H. R.

Co-PIs: Goodwin, D. C., Suh, S.-J., Hamid, A.,

Dates:  6/01/20 - 5/31/22

Mapping the Metabolic Impact of Sulfur Limitation on the Terrestrial Microbiome

Amount: $435,212.14

            Contribution: Effort 15%; Funds ~15% Drs. Ellis and Goodwin co-advise a graduate whose support is proposed in this application.

(Submission Deadline: March 2, 2020)

 

National Institutes of Health (NIAID R15 AI147315-01)

PI: Goodwin, D.C.

Co-I: Calderón, A.

Dates:  6/01/19 - 5/31/21

Strategies to identify and assess chemical probes against mycobacterial shikimate kinase: From mechanisms of inhibition to metabolomics.

Amount: $437,404

 

National Institutes of Health (NAID R15 AI113684-01A1)

PI’s:  Calderón, A.I., Goodwin, D. C.

Submitted:  10/25/17

Title: Strategies for uncovering selective and mechanistically appropriate natural product inhibitors of Mycobacterium tuberculosis shikimate kinase.

Amount:  $438,313

            Contribution: Effort 50%; Funds ~40% (See note under 4.2.g.1 Planned for Submission)

 

National Institutes of Health (NAID R15 AI113684-01A1)

PI’s:  Calderón, A.I., Goodwin, D. C.

Submitted:  06/25/15

Title: Toward New Antitubercular Drugs: Uncovering Mechanistically Appropriate Inhibitors of Mycobacterium tuberculosis Shikimate Kinase from Natural Products

Amount:  $437,931

            Contribution: Effort 50%; Funds ~40% (See note under 4.2.g.1 Planned for Submission)

 

National Science Foundation (MCB 1517433)

PI:  Goodwin, D. C.

Submitted:  11/17/14

Title:  Maximizing Cellular Resistance to Hydrogen Peroxide: Synergy Between KatG Activities

Amount:  $523,259

 

National Science Foundation (MRI 1429654)

PI:  Mansoorabadi, S.

Co-PI’s: Duin, E.C., Ellis, H.R.

Role: Contributed to the proposal as a major user/collaborator

Submitted:  01/23/14

Title:  Acquisition of a Rigaku Protein Structure Workbench

Amount:  $694,756

 

National Institutes of Health (NIAID R15 AI113684)

PI’s:  Calderón, A.I., Goodwin, D.C.

Submitted: 10/25/13

Title: Toward New Antitubercular Drugs: Uncovering Mechanistically Appropriate Inhibitors of Mycobacterium tuberculosis Shikimate Kinase from Natural Products

Amount:  $444,000

Contribution: Effort 50%; Funds ~40% (See note under 4.2.g.1 Planned for Submission)

 

National Science Foundation (CLP 1306931)

PI: Goodwin, D. C.

Submitted: 10/31/12

Title: Synergy Not Antagonism in Antioxidant Defenses: How Peroxidatic Electron Donors Make KatG a Novel and More Efficient Catalase

Amount: $539,972

 

National Science Foundation (CLP 1214099)

PI: Goodwin, D. C.

Submitted: 11/30/11

Title:  Enlisting Peroxidatic Electron Donors to Exapand the Catalytic Activity of KatG: Implications for the Baterial Response to Hydrogen Peroxide

Amount: $525,555

 

National Science Foundation (DUE 0728674)

PI: Marcy, R.

Co-PI’s: Newton, S., Armstrong, A., Long, V., Goodwin D. C.

Submitted: 02/16/07

Title: ASCC: Adaptive, Science, Customization, Curriculum

Amount: $597,243

 

National Science Foundation (DBI 0649881)

PI: Hong, J.W.

Co-PI: Goodwin D. C.

Submitted:  08/25/06

Title: Development of a Novel Protein Kinetics Landscaper for Biological Catalysis

Amount: $383,720

Contribution: 25%

 

National Science Foundation (MCB 0516905)

PI: Goodwin, D. C.

Submitted: 01/12/05

Title: Vital Roles of an “Inactive” Domain in Catalase-peroxidase Catalysis

Amount: $398,308

 

National Science Foundation (MRI 0521180)

PI: Shannon, C.

Co-PI’s: Cheng, Z., Prorok, B., Goodwin D. C., Park, M.

Submitted: 01/27/05

Title: A Raman Spectroscopy User Facility at Auburn University

Amount: $445,000

 

National Institutes of Health (R01 GM069638-01A1)

PI: Goodwin, D.C.

Submitted: 03/01/04

Title: Vital Role of an Inactive Domain in Catalase-Peroxidases

Amount: $572,242

Contribution: Effort 50%; Funds ~40% (See note under 4.2.g.1 Planned for Submission)

 

National Science Foundation (MCB 0417109)

PI: Goodwin, D. C.

Submitted: 01/12/04

Title: Vital Roles of an “Inactive” Domain in Catalase-peroxidase Catalysis

Amount: $369,168

 

National Institutes of Health (R01 GM069638-01)

PI: Goodwin, D.C.

Submitted: 02/01/03

Title: Vital Role of an Inactive Domain in Catalase-Peroxidases

Amount: $572,242

 

National Science Foundation (MCB 0315894)

PI: Goodwin, D. C.

Submitted: 01/10/03

Title: Vital Roles of an Inactive Domain in Catalase-peroxidase Catalysis

Amount: $285,089

 

National Institutes of Health (R15 DK60500)

PI: Goodwin, D. C.

Submitted: 01/17/10

Title: ONOO^- Reduction by E. coli O157:H7 Catalase-Peroxidase

Amount: $143,000

 

National Science Foundation (MRI 0078857)

PI: Albrecht-Schmitt, T.A.

Co-PI’s: Goodwin, D.C., Cammarata, V., Schevlin, P., Stanbury, D.M.

Submitted: 01/13/00

Title: Acquisition of a single crystal X-ray diffractometer for structural studies on new materials, small molecules and biomolecules

Amount: $203,490

 

 

 

 

4.B.g.2. Internal Sources

 

Intramural Grants Program

PI: Calderón, A.

Co-PI: Goodwin, D.C.

Dates: 3/1/13 – 2/28/15

Title: Toward new antitubercular drugs: Uncovering mechanistically appropriate inhibitors of Mycobacterium tuberculosis shikimate kinase from natural products

Amount: $54,000

 

Promoting Research in Sciences and Mathematics (PRISM), COSAM

PI: Goodwin, D. C.

Co-PI’s: Ellis, H.R., Singh, N., Duin, E.

Dates: 03/20/04 – 03/19/05

Title: Circular dichroism at Auburn University (Externally Reviewed)

Amount: $100,000

 

Auburn University Biogrants Program

PI: Goodwin, D. C.

Dates: 05/01/01 – 09/30/03

Title: Mechanisms of heme acquisition by enterohemorrhagic E. coli strain O157:H7 (Externally Reviewed)

Amount: $20,323

 

Dean’s Research Initiative Grant, COSAM

PI: Goodwin, D. C.

Dates: 11/01/00 – 10/31/01

Title: Mechanisms of heme acquisition by pathogenic bacteria.

Amount: $10,000.

 

Competitive Research Grant, Office of the Vice President for Research

PI: Goodwin, D. C.

Dates: 05/01/00 – 04/30/01

Title: Function of catalase-peroxidase from Enterohemorrhagic Escherichia coli O157:H7.

Amount: $10,000

 

Small Equipment Grant, Office of the Vice President for Research

PI: Goodwin, D.C.

Dates: 10/01/99 – 09/30/00

Title: Proposal for the Purchase of an Ultralow Freezer for the Storage of Temperature Sensitive Biochemical Research Materials

Amount: $4,797

 

            New Faculty Start-Up, Department of Chemistry/COSAM/OVPR

            PI: Goodwin, D.C.

            Dates: 10/01/99 – 09/30/02

            Amount: $160,000

 

4.B.g.3. Other

 

      Dr. G. Lynn and Cheryl Marks Family Scholarship for Undergraduate Research

A donation from the Marks family and matched by GlaxoSmithKline was established and earmarked specifically to support an undergraduate student each year working on M. tuberculosis related proteins in my laboratory. The scholarship pays a stipend to the student of between $1,000 and $2,000 for the year.

 

Marks Scholars

 

Student	Major	Dates	Post Auburn
Erin Wilkinson	Biochemistry	08/25 – present
Jada Conner	BA Chemistry	08/24 – present
Louisa Forbes	Biochemistry	08/23 – present
Ryan Mumford	Biochemistry	08/21 – 5/23	MD, USA
Nina Orihuela	BA Chemistry	08/21 – 5/22	MD, UAB
Aishah Lee	Biochemistry	08/20 – 05/21	Evonik
Laura Minton	Biomed Sci	08/19 – 05/20	MD, UAB
Savannah Petrus	Biochemistry	08/18 – 05/19	MD, UAB
Patrick Sahrmann	Biochemistry	08/16 – 05/18	PhD, U. Chicago
Olivia Snider	Biochemistry	08/15 – 05/16
Lauren Barr	Biomed Sci	08/14 – 05/15	MD, Vanderbilt

 

4. C.   OUTREACH

 

4.C.a.  Commentary

 

Prison Education Outreach

 

With nearly 570 prisoners per 100,000 residents, Alabama has the ninth highest incarceration rate in the United States, a statistic made more alarming by the fact that the United States has the highest incarceration rate in the world. There are nearly 28,000 prisoners in the Alabama Department of Corrections (ADOC) system.¹ At the same time, opportunities for prisoners to better themselves through education remain extremely limited. Despite the well-documented benefits of educational programs for prisoners, their families, and their communities, only about 2% of the ADOC prison population is involved in educational programming of any kind. Having successfully implemented several arts and humanities courses, the Alabama Prison Arts + Education Project (APA+EP) sought to address the pressing need for and very strong interest of prison-based students in STEM education opportunities. The SPARKs in Science and Mathematics lecture series was one avenue by which the APA+EP sought to pursue this objective. SPARKs is a seminar series presented by Auburn University faculty from the Colleges of Sciences and Mathematics, Agriculture, and Engineering. Participating faculty each present a single lecture on the area of their expertise in an ADOC facility. Over a 10 – 12 week series, a broad and engaging set of topics are vigorously engaged by the students, serving to pique the interest of students in pursuing additional education in the STEM courses that the APA+EP continues to develop.

 

I gave my first SPARKs series talk in Spring 2012, and I was won over by a great group of highly engaged students. I received so many questions from the students that an hour of

prepared material took the full two-hour seminar period to cover. That experience changed my life. I was won over by the enthusiasm and engagement of the students so much so that I then not only participated in SPARKs every year, but I sought to recruit as many of my colleagues to participate as possible.

1Hinds, O. et al. People in Prison 2017. Vera Institute of Justice, https://www.vera.org/publications/people-in-prison-2017

 

The impact of the SPARKs emanates in multiple directions to the benefit of APA+EP students and teachers, alike. First, the students have the opportunity to engage discussions in STEM topics that they might not encounter otherwise. As one of our students has said, “These [lectures] are more exciting because they all take me to places I’ve never thought of.” As importantly, material presented in the prison classroom never remains contained within that space. Rather, the material is discussed and shared with others who were not in attendance, contributing positively to the education (formal and informal) of others. With respect to an impact on other formal educational programs, one of our students has reported, “I teach pre-GED on Tuesdays and Thursdays and will share some of the General Education materials with the students.” Likewise, by less formal (but no less important) mechanisms, another of our students has written, “These classes have become well known in the camp and the younger men are becoming interested and that’s a good thing, getting them to think in another direction. Those that attend find that they have constructive conversations rather than those of the convict mentality.”

 

Participation in SPARKs has had a profound impact on me and my teaching, and as a result, has been a benefit to the Auburn University students who come through my courses. First, participation in APA+EP has changed the way I think about prisons, criminal justice reform, and most of all, the many APA+EP students seeking to better themselves through education. Second, teaching in prison-based ‘classrooms’ has done more to spur innovation and creativity in my own teaching than anything else I have done. Although technology can enable teachers to engage students in ways not possible even a few years ago, it is important to recognize that the use of technology is not necessarily the same thing as innovation. Indeed, it is precisely the limitations imposed by the prison ‘classroom’ that have produced some of the most notable changes to my teaching in the university setting. For example, there is no internet access, and it is a felony to carry a cell phone into a prison. In addition, one is confronted with a greatly varied audience in terms of background in the subject. One must find ways to effectively bring the material across to an audience where some of the students present may never have finished sixth grade and others may have Master’s degrees and/or some professional school training. My experiences in SPARKs have made me a better communicator of challenging concepts in my university classrooms. The Molecular Players Theater where I enlist the assistance of students to help me physically act out complex mechanisms was developed in large part through my SPARKs presentations. It is about as low-tech as one could possibly get. For example, the classroom space comes to represent the separation between active sites in the pyruvate dehydrogenase complex, student ‘volunteers’ become cofactors as identified by the paper placards they carry, steps like decarboxylation are manipulations (e.g., literally tearing) of paper representations of substrates, and the channeling of intermediates from one active site to the next has me running from one end of the classroom to the other. By way of the feedback I receive from them in formal teaching evaluations and in informal conversation, these are the kinds of things that my Auburn University students remember most about their time in my courses.

 

Finally, it is important to mention that innovations also carry the other way (i.e., Auburn to prison classroom), albeit at a slower, security-limited pace. In my most recent SPARKs presentation, I was able to take materials into the facility to carry out various aspects of the peroxidase demonstration for the students. In this way, SPARKs model is one that may be particularly effective in enabling expansion of what is allowed in the prison classroom. By individual faculty presenters going through what is necessary to try a new approach in a

single lecture, prison administration is able to observe, on a small scale, that the activity in question can be carried out while minimizing risks to security. The expectation is that these small steps will pave the way for future prison classroom innovations.

 

Summer Bridge: Building Awareness of and Engagement in Undergraduate Research

 

The Summer Bridge Program is designed to assist incoming COSAM freshmen who are from groups underrepresented in STEM careers to make the transition to the collegiate environment. It is a Summer mini-mester of courses that provides foundational content that facilitates success in navigating the challenging courses of COSAM curricula. The program also teaches effective study habits and time-management skills to help increase success in undergraduate study, ultimately leading to graduation.

 

Data are showing that undergraduate research experiences provide a myriad of benefits to the students who participate.² I have come to the same conclusions by observing the undergraduates who have worked in my laboratory. Participation in undergraduate research, then, represents a powerful instrument that aligns well with the objectives of the Summer Bridge program. Together, my colleague, Dr. Holly Ellis, and I developed a two-part contribution to the Summer Bridge program designed to increase awareness of and participation in undergraduate research.

 

Research Q and A. The purpose of this session/lecture is to encourage participation of these incoming undergraduates in research programs as their academic programs progress. It is anticipated that promotion of research activities to Summer Bridge participants as they enter the university will lead to their application for fellowships later in their undergraduate programs.

 

Hands on undergraduate research demonstration. Students participate in a redox biochemistry experiment based on peroxidase chemistry. The results are visually colorful/striking. The exercise is a fun way to get pipettors in hand, propose and perform a short experiment, and evaluate the results. Importantly, among the materials used are modified enzymes originally produced by undergraduate researchers in the Goodwin Laboratory (e.g., Robert Campbell’s KatG[D209-228]).³

 

Applications of the Peroxidase Demonstration

 

      As mentioned above and illustrated in previous sections (4.A.g Other Contributions to Teaching), the peroxidase system is highly adaptable to a wide range of educational applications. It can be used as a front-of-classroom demonstration of multiple chemical/biochemical concepts (e.g., enzyme catalysis, redox titration, free-radical chemistry, anti-oxidant properties of foods and vitamins, etc.). Similarly, in outreach activities like Summer Bridge, this system is adaptable to hands-on activities of varying depth and complexity, depending on the time available and the goals of a given program. An added attractive feature of this system is its versatility in terms of the materials that can be used and the relatively low cost of purchasing them. As such, I have adapted this system for use by students in Science Olympiad or Teaching Enhancement Award activities, and even at home with commonly available materials.

 

2Lopatto, D. Undergraduate Research as a High-Impact Student Experience. 2010. Peer Review 12. AACU 3Kudalkar, S.N., et al. J. Inorg. Biochem. 116, 106 – 115.

 

4.C.b.  Activities and Products

 

4.C.b.1.  Instructional Activities

 

Prison-based education: SPARKs in Science and Mathematics

 

SPARKS in Science and Mathematics, Faculty Prison Lecture Series Seminar

Title: Proteins, radicals, vitamins, and minerals: How biology makes metabolism work.

Duration: 2 hours classroom time; 2.5 hours drive time; 1 hour security check-in

Audience: APA+EP students of Tutwiler Correctional Facility, Wetumpka, AL.

Method: In-person site visit, lecture, demonstration, and Q and A

Date: 03/30/22

Role: Material/Demonstration Developer and Presenter

 

Organizing faculty presenters for prison lecture series

Title: SPARKS in Science and Mathematics

Duration: 20 hours soliciting presenters and preparing presentation schedule

Audience: APA+EP students of Tutwiler Correctional Facility, Wetumpka, AL.

Method: e-mail communication

Dates: 10/01/21 – 01/30/22 (Initial e-mail thru faculty presenter security training)

Role: Faculty organizer

 

SPARKS in Science and Mathematics, Faculty Prison Lecture Series Seminar

Title: Proteins, radicals, vitamins, and minerals: How biology makes metabolism work.

Duration: 2 hours classroom time; 2.5 hours drive time; 1 hour security check-in

Audience: APA+EP students of Ventress Correctional Facility, Clayton, AL.

Method: In-person site visit, lecture, demonstration, and Q and A

Date: 03/06/19

Role: Material/Demonstration Developer and Presenter

 

Organizing faculty presenters for prison lecture series

Title: SPARKS in Science and Mathematics

Duration: 20 hours soliciting presenters and preparing presentation schedule

Audience: APA+EP students of Ventress Correctional Facility, Clayton, AL.

Method: e-mail communication

Dates: 10/01/18 – 01/30/19 (Initial e-mail thru faculty presenter security training)

Role: Faculty organizer

 

SPARKS in Science and Mathematics, Faculty Prison Lecture Series Seminar

Title: Proteins, radicals, vitamins, and minerals: How biology makes metabolism work.

Duration: 2 hours classroom time; 2.5 hours drive time; 1 hour security check-in

Audience: APA+EP students of Staton Correctional Facility, Elmore, AL.

Method: In-person site visit, lecture, demonstration, and Q and A

Date: 04/20/18

Role: Material/Demonstration Developer and Presenter

 

Organizing faculty presenters for prison lecture series

Title: SPARKS in Science and Mathematics

Duration: 20 hours soliciting presenters and preparing presentation schedule

Audience: APA+EP students of Staton Correctional Facility, Elmore, AL.

Method: e-mail communication

Dates: 09/15/17 – 01/26/18 (Initial e-mail thru faculty presenter security training)

Role: Faculty organizer

 

SPARKS in Science and Mathematics, Faculty Prison Lecture Series Seminar

Title: How cells make molecules that work: Sensors, pumps, motors, and power generators.

Duration: 2 hours classroom time; 2.5 hours drive time; 1 hour security check-in

Audience: APA+EP students of Tutwiler Correctional Facility, Wetumpka, AL.

Method: In-person site visit, lecture, demonstration, and Q and A

Date: 03/13/17

Role: Material/Demonstration Developer and Presenter

 

Organizing faculty presenters for prison lecture series

Title: SPARKS in Science and Mathematics

Duration: 20 hours soliciting presenters and preparing presentation schedule

Audience: APA+EP students of Tutwiler Correctional Facility, Elmore, AL.

Method: e-mail communication

Dates: 11/4/16 – 02/06/17 (Initial e-mail thru faculty presenter security training)

Role: Faculty organizer

 

SPARKS in Science and Mathematics, Faculty Prison Lecture Series Seminar

Title: How cells make molecules that work: Sensors, pumps, motors, and power generators

Duration: 2 hours classroom time; 3.5 hours drive time; 1 hour security check-in

Audience: APA+EP students of Easterling Correctional Facility, Clio, AL.

Method: In-person site visit, lecture, demonstration, and Q and A

Date: 03/28/16

Role: Material/Demonstration Developer and Presenter

 

Organizing faculty presenters for prison lecture series

Title: SPARKS in Science and Mathematics

Duration: 20 hours soliciting presenters and preparing presentation schedule

Audience: APA+EP students of Easterling Correctional Facility, Clio, AL.

Dates: 11/01/15 – 02/12/16 (Initial e-mail thru faculty presenter security training)

Role: Faculty organizer

 

SPARKS in Science and Mathematics, Faculty Prison Lecture Series Seminar

Title: Protein structure and function: Building and managing catalysts for life

Duration: 2 hours classroom time; 2.5 hours drive time; 1 hour security check-in

Audience: APA+EP students of Staton Correctional Facility, Elmore, AL.

Method: In-person site visit, lecture, demonstration, and Q and A

Date: 02/26/15

Role: Material/Demonstration Developer and Presenter

 

Organizing faculty presenters for prison lecture series

Title: SPARKS in Science and Mathematics

Duration: 20 hours soliciting presenters and preparing presentation schedule

Audience: APA+EP students of Staton Correctional Facility, Clio, AL.

Method: e-mail communication

Dates: 11/04/14 – 02/04/15 (Initial e-mail thru faculty presenter security training)

Role: Faculty organizer

 

Special Grant Program in Chemical Sciences (preproposal)

The Camille and Henry Dreyfus Foundation, Inc.

PI: Goodwin, D.C.

Co-PI: Shannon, C.

Title: Expanding educational opportunity through chemistry

Duration: 09/01/14 – 08/31/15

Amount: $27,400

Description: The project was to establish a chemistry course for an ADOC facility drawing on departmental faculty teaching expertise course and a general science course for Alabama Prisoners using iPads as a foundational teaching tool. In addition, the grant was to support a SPARKs lecture series, and establish the SPARKs II-type lecture series.

 

SPARKS in Science and Mathematics, Faculty Prison Lecture Series Seminar

Title: Protein structure and function: Building and managing catalysts for life

Duration: 2 hours classroom time; 2.5 hours drive time; 1 hour security check-in

Audience: APA+EP students of Elmore Correctional Facility, Elmore, AL.

Method: In-person site visit, lecture, demonstration, and Q and A

Date: 02/13/14

Role: Material/Demonstration Developer and Presenter

 

Guide for new prison lecture faculty

Title: SPARKS in Science and Mathematics

Duration: 2 hours classroom time; 2.5 hours drive time; 1 hour security check-in for each of three presentations

Audience: APA+EP students of Elmore Correctional Facility, Elmore, AL.

Method: Accompanied three new faculty presenters to assist with security check-in, etc.

Dates: March 6 (C. Bailey, presenter), April 3 (J. Feminella and B. Helms, presenters), and April 10, 2014 (S. Rodning, presenter)

 

SPARKS in Science and Mathematics II, Faculty Prison Lecture Miniseries

Seminar Title: Building biology from the ground up: Atoms to molecular pumps and power generators (3-part series)

Duration: 2 hours classroom time; 3.5 hours drive time; 1 hour security check-in for each of three trips; 7 hours PREA and security training (01/07/14)

Audience: APA+EP students of Easterling Correctional Facility, Clio, AL.

Method: In-person site visit, lecture, demonstration, and Q and A

Dates: February 12, 19, and 26, 2014

Role: Material/Demonstration Developer and Presenter

 

Auburn University Competitive Outreach Grant

PI: Stevens, K., APA+EP Director

Co-PIs: Goodwin, D. C., and Wilson, A.

Title: Bridging the curriculum gap in prisoner education: A collaboration of colleges

Duration: March 1, 2013 – February 28, 2014

Amount: $59,568

Description: The purpose of the grant was to establish a mathematics course and a general science course for Alabama Prisoners using iPads as a foundational teaching tool. In addition, the grant was to support a SPARKs lecture series, and establish the SPARKs II-type lecture series.

 

SPARKS in Science and Mathematics, Faculty Prison Lecture Series Seminar

Seminar Title: Building Biology from the Ground Up: Atoms to Molecular Pumps and Power Generators

Duration: 2 hours classroom time; 2.5 hours drive time; 1 hour security check-in

Audience: APA+EP students of Elmore Correctional Facility, Elmore, AL.

Method: In-person site visit, lecture, demonstration, and Q and A

Date: March 12, 2012

Role: Material/Demonstration Developer and Presenter

 

Summer Bridge Program

 

Hands-on undergraduate research demonstrations

Laboratory Title: Enzyme catalysis, free radicals, and antioxidants

Duration: 2 hours presentation/laboratory time; 12 hours preparation time (each date)

Audience: Students of the COSAM Summer Bridge Program

Method: Laboratory technique demonstration, scientific foundation/exposition, and experiment supervision

Dates: June 23, 2016; June 11, 2015; June 17, 2014; June 16, 2013; June 20, 2012.

Role: Primary organizer, lecturer, and supervisor

Assistance: Typically, two graduate students and two undergraduate students

 

Undergraduate research/research career question and answer session

Session Title: Enhancing your undergraduate education and experience through research

Duration: 1 hour presentation time; 2 hours preparation time (each date)

Audience: Students of the COSAM Summer Bridge Program

Method: Co-led Q and A session with Dr. Holly Ellis

Dates: June 6, 2017, June 10, 2015; June 13, 2014; June 15, 2013; June 13, 2012.

Role: Co-organizer and co-lecturer

 

Teaching Enhancement Award Activities

 

TEA 2009

Activities: High school student research training (two weeks); High school teacher co-training (one week); closing presentation preparation and delivery.

Project Title: Antioxidants: Totally rad!

Duration: Three 40-hour weeks

Participants: Kendall Hall (HS Student); Lynn McCain (HS Teacher)

Dates: June 2009

Role: Identified, set up, and directed the research project, trained the student in laboratory techniques, data collection, and data analysis, advised on poster construction and final oral presentation.

 

TEA 2007

Activities: High school student research training (two weeks); High school teacher co-training (one week); closing presentation preparation and delivery.

Project Title: Radical approach to evaluating and teaching kinetics of antioxidants

Duration: Three 40-hour weeks

Participants: W.C. “Dub” Davison (HS Student); Warren Hamm (HS Teacher)

Dates: June 2007

Role: Identified, set up, and directed the research project, trained the student in laboratory techniques, data collection, and data analysis, advised on poster construction and final oral presentation.

 

Other Instructional Activities

 

Alabama Science and Engineering Fair

Activity: Best of Fair Judge; evaluated top candidates submitted by Head Category Judges for Best of Fair awards, deliberated with other Best of Fair Judges to down-select six finalists, panel review to select four finalists.

Duration: 6 hours (day of event)

Dates: April 1, 2023

 

 

 

Science Olympiad

Activity: Represented the Department of Chemistry and Biochemistry, assisting Mary Lou Ewald and Dr. Allen Lander (Chair, Department of Physics) in the distribution of awards for Science Olympiad Events.

Duration: 2 hours (day of event)

Dates: March 26, 2022

 

Kitchen Biochemistry

Activity: Devised and implemented a set of experiments in enzyme isolation and kinetic evaluation using materials commonly available at the grocery store (horseradish root, hydrogen peroxide, vinegar, liquid laundry detergent, etc.). 

Duration: Three 1-hour in-laboratory sessions; 4 hours communication/direction regarding the home/kitchen experience

Dates: Spring 2011

Role: Provided instruction to home school students for performing experiments and making qualitative evaluations in their own kitchens. Instructed students in the lab setting using advanced reagents and instruments to do parallel experiments.

 

Middle School Science Olympiad

Duration: 10 hours (day of event); 30 hours preparation

Dates: February 28, 2009

Role: Chemistry section co-organizer (with Dr. Holly Ellis); Co-Event Supervisor (Experimental Design)

 

Middle School Science Olympiad

Duration: 5 hours (day of event); 20 hours preparation

Dates: March 2008

Role: Developed and implemented Food Science event

 

Community College Instructor Laboratory Training

Participant: Dr. Ronald Marcy, Division Chair, Biology and Chemistry, Alabama Southern Community College. 

Duration: Several Saturdays over the Spring semester of 2003.

Role: Supervised training for Dr. Marcy in the Goodwin laboratory learning techniques, including site-directed mutagenesis, recombinant protein expression, protein purification, and enzymatic characterization. He then used this information to alter lecture and laboratory courses at his home institution.

 

4.C.b.2. Technical Assistance

 

Destination STEM

Date: September 22, 2017

Participants: Rene Fuanta and Dianna Forbes (Chemistry and Biochemistry graduate students) as demonstrators for middle and HS students

Duration: 10 hours pre-event consultation and instruction

Role: Trained and consulted with Rene and Dianna on the set-up and execution of their peroxidase-based demonstration of free radical chemistry.

 

 

4.3.b.5. Other Outreach Products        

 

COSAM Outreach in Prison

A seminar on the APA+EP to the COSAM Leadership Council

Date: October 2, 2015

            Attendees: COSAM Leadership Council members and other stakeholders

            Duration: 30 minutes

            Role: Speaker

 

Promotional video for the APA+EP

            Dates: April 7, 2014 (interview shooting); November 2014 video review

Participants: Stevens, K., APA+EP Director

Beal, A., and Goodwin, D.C., APA+EP instructors

Duration: 4 hours total for interview and editorial review

Role: Interviewee

Link: Final video product (published December 1, 2014)

 

2014 AU Outreach Symposium (team presentation)

Title: Bridging a Curriculum Gap in Prisoner Education

Date: February 11, 2014

Participants: Stevens, K., APA+EP Director

Goodwin, D.C., Wilson, A., and Beal, A., APA+EP instructors

Duration: 1 hour presentation; 5 hours preparation

Role: Co-presenter

 

4.C.b.6. Outreach Grants

 

Auburn University Competitive Outreach Grant

PI: Stevens, K.

Co-PIs: Goodwin, D.C.; Wilson, A.

Dates:  3/1/13 – 2/28/14

Title: Bridging the Curriculum Gap in Prisoner Education: A Collaboration of Colleges Innovating Solutions

Amount: $59,568

 

 

 

4. D.  SERVICE

 

4.D.a. University Service (Current in Italics)

 

4.D.a.1. Department of Chemistry and Biochemistry Service:

 

Department Chair, Department of Chemistry and Biochemistry, Auburn University, 07/20 – present.

 

Member, Chemistry and Biochemistry Leadership Council, 09/18 – present.

 

Faculty Advisor, NOBCChE Auburn University Student Affiliate, Department of Chemistry and Biochemistry, 05/23 – present.

 

Member, COSAM Dean Search Committee (Department Chairs’ representative) 11/20 – 04/21.

 

Member, COSAM Dean Search Committee (Department Chairs’ representative) 11/20 – 04/21.

 

Presenter, Graduate Student Recruiting Invitational, Chemistry and Biochemistry, 11/08/19. Graduate School 101

 

Graduate Program Officer, 05/17 – 06/20.

Special Project, Graduate Handbook Major Revision, 01/20 – 06/20. Included implementation of committee-based annual reviews of graduate students, adoption of department-level Plan of Study procedures and protocols, enhanced mechanisms for committee selection, and institution of graduate student representatives.

 

Special Project, Graduate Handbook Major Revision, 02/18 – 10/18. Included substantial policy revisions, implementation of assessment procedures and instruments, soliciting DBC faculty and graduate student input, and obtaining faculty approval of individual components and the final Graduate Handbook.

 

Chair, Graduate Program Committee, 05/17 – 06/20.

 

Chair, Biochemistry Division, 05/05 – 05/19.

 

Developer, General Doctoral Exam (written and oral) assessment rubrics

 

Manager, CD Spectropolarimeter, 06/04 – present.

 

Chair, Graduate Admissions Committee, 01/10 – 05/17.

 

Member, Graduate Recruiting/Visits/Admissions Committee, 08/06 – 12/09.

 

Member, Graduate Student Admissions Committee, 09/99 – 07/06.

 

Chair, Biological Instrumentation Committee, 08/06 – 05/09.

 

Manager, MALDI Mass Spectrometer, 09/04 – 05/09.

 

Member, Faculty Search Committee, Bioimaging and Biochemistry, 08/16 – 02/17. (Raj)

 

Chair, Biochemistry Faculty Search Committee, 08/11 – 05/12. (Mansoorabadi)

 

Member, Physical Chemistry Faculty Search Committee, 9/09 – 12/10. (Patkowski)

 

Member, Departmental Faculty Council, 08/06 – 08/09.

 

Coordinator, Chemistry and Biochemistry Colloquium Program, 08/05 – 05/09.

 

Colloquium funding obtained:

Increasing the Caliber and Diversity of Chemistry and Biochemistry Colloquium COSAM; $37,500; 1/1/06 – 5/1/08.

 

Presenter, Faculty research synopses, ACS Auburn Section Student Affiliate, 02/19/09.

 

Presenter, Graduate Student Recruiting Invitational, Chemistry and Biochemistry, 01/09.

 

Member, Department of Chemistry Chair Search Committee, 06/2005 – 01/06. (Ortiz)

 

Graduate Student Recruiter, Southeast Regional Meeting of the American Chemical Society (SERMACS), Raleigh 11/04, Atlanta 11/03, Charleston 11/02, Savannah 09/01.

 

Member, Biological NMR Faculty Search Committee, 08/03 – 12/04. (Mohanty)

 

Organizer, State University of West Georgia REU Visit to Auburn Chemistry and Biochemistry, 12 undergraduates, 1 faculty, 06/13/03.

 

Chair, Biochemistry Faculty Search Committee, 07/01 – 05/02. (Duin)

 

Chair, Biomacromolecular Crystallography Faculty Search Committee, 07/00 – 05/01.

 

Member, Biochemistry Faculty Search Committee, 07/00 – 05/01. (Ellis)

 

Member, Biochemistry Faculty Search Committee, 08/99 – 05/00).

 

Academic Advisor, Biochemistry Majors, Chemistry and Biochemistry, 08/00 – 05/17.

 

 

Academic Advisees

Major	Students (46 total)
Biochemistry	Jessica Andry, Daniel Arias , Austin Arnold, Kendal Benson, Christy Bronaugh, Matthew Brown, Bryan Cronin, Jennifer Falls, Eric Funderburg, Carmen Gaines, Grayson Gladdish, Timothy Guice, Morgan Gwynn, Kathryn Heflin, Kristen Hertwig, Graham Johnson, Kelly Lynn, Cecilia Masucci, Matthew McDonald, Walter Meadows, JaRyce Nabors, Natasha Narayanan, Mary O’Barr, Aseba Okim, Thomas
	Parish, Sarah Peaslee, Alexander Pilgreen, John Rinker, Bailey Roberts, Tyler Sharp, Gary Sheffield, Daniel Smith, Tanner Smith, Molly Smithers, Andrew Stephens, Ashleigh Stokes, Cameron Terrell, Ryan Tucker, William Walraven, Rachel Williams, Landon Wilson, Carl Worley, Jeffery Zaballa
Chemistry	Jenny Alexander, David Hagins
Molecular Biology	Emily Brantley

 

 

4.D.a.2. COSAM Service:

 

Member, COSAM Executive Team, 07/20 – present.

 

Member, COSAM Biomedical Sciences Advisory Committee, 01/24 – present.

 

Member, COSAM Biomedical Sciences Program Review Committee, 03/23 – 11/23.

 

Chair, COSAM Associate Dean for Research and Graduate Affairs Search Committee (March – April 2023)

 

Member, COSAM Acting Deputy Associate Dean for Academic Affairs Search Committee (April – May 2022)

 

Member, COSAM Acting Associate Dean for Research Search Committee (July 2021)

 

Member, COSAM Dean Search Committee (August 2021 – April 2022).

 

Member, COSAM Dean Search Committee (November 2020 – April 2021).

 

Member, Cellular and Molecular Biosciences Program Graduate Fellowship Committee, (Spring 2007, Spring 2008, Spring 2009).

 

Member, Dean’s Research Awards Committee, 08/06 – 05/09.

 

Member, COSAM Leaders Faculty/Student Interview Panel, 04/04, 04/05 04/07, 04/08.

 

            Member, Biological NMR Symposium Organizing Committee, 08/02 – 05/03.

 

 

4.D.a.3. University Service

                       

Member, Advisory Workgroup on Faculty Compensation, Workload, and Productivity, 10/24 – present.

 

Member, Advisory Council, Alabama Prison Arts + Education Project, 09/15 – present.

 

Chair, Academic Administrator Review Committee, Mechanical Engineering, 09/24 – 03/25.

 

Member, Academic Program Review, Auburn University-based Panel Member, Crop, Soil, and Environmental Sciences, College of Agriculture, 01/21 – 05/21.

 

Senator, Chemistry and Biochemistry representative to the University Senate, 07/15 – 07/20.

 

Member, Project Coordinator Search Committee, Alabama Prison Arts + Education project, 09/16 – 04/17.

 

Member, Ad Hoc Mock Interview Panel, Gates-Cambridge Finalist, 01/14 – 02/14.

 

Faculty Representative, Camp War Eagle Session 4, 06/25/15 – 06/26/15.

 

4.D.b. Professional Service

 

Representative (05/2023 – present), NOBCChE Collaborative (Charter 1), represent Auburn University in NOBCChE activities toward development of STEM faculty from underrepresented groups. Affiliated institutions included Auburn University, Hampton University, Jackson State University, Ohio State University, University of Pittsburg, and Winston Salem State University

 

Program Chair, 11^th Annual Southeast Enzyme Conference, originally scheduled May 16, 2020 and postponed to April 10, 2021, Virtual.

 

Reviewer,  Biochemistry, Journal of the American Chemical Society, Biochimica et Biophysica Acta, General Subjects, Biochimica et Biophysica Acta, Proteins and Proteomics, Journal of Biological Inorganic Chemistry, Biochemie, Journal of Inorganic Biochemistry, Journal of Biological Chemistry, Chemical Research in Toxicology, Biophysical Chemistry, PLOS One, Proceedings of the National Academy of Sciences, Phytochemistry Reviews, Bioorganic and Medicinal Chemistry, Applied Microbiology, International Journal of Chemical Kinetics

 

Ad Hoc Reviewer (2007 - present), National Science Foundation

 

Lead Panelist, National Science Foundation, Metabolic Biochemistry Panel, Fall 2009 – four proposals.

 

Secondary Panelist, National Science Foundation, Metabolic Biochemistry Panel, Fall 2009 – four proposals.

 

Scribe Panelist, National Science Foundation, Metabolic Biochemistry Panel, Fall 2009 – four proposals.

 

Lead Panelist, National Science Foundation, Metabolic Biochemistry Panel, Fall 2008 – six proposals.

 

Secondary Panelist, National Science Foundation, Metabolic Biochemistry Panel, Fall 2008 – six proposals.

 

Session Chair, Fifth Southeast Enzymes Conference, Atlanta, GA, 04/05/14

 

Treasurer, American Chemical Society, Auburn Section, 02/00 – 03/04

 

Member, American Chemical Society, Division of Biological Chemistry

 

Member, American Society for Biochemistry and Molecular Biology

 

4.D.c. Other

 

Letters, because I have taught courses with large numbers of undergraduate students close to graduation, I have written a very large number of recommendation letters every year. Over the last eight years, I have written 583 letters for 265 different students and colleagues.