Jessica Krewall

Jessica came to Auburn University in August 2015, and she joined the Goodwin Laboratory in January 2016.  Originally, from Colorado Springs, she came to us by way of Wayland Baptist University in Plainview, TX. So, not only did she and Doc hail from the same town, but Jessica carried out her research under the supervision of Dr. Robert Moore.  Yes, that Robert Moore.  After completing his PhD here at Auburn, Dr. Moore joined the faculty at Wayland. Jessica was a star student in the classroom and in the lab at Wayland, so we were very glad to have her here. In the Goodwin Lab, Jessica evaluated mechanisms of KatG catalysis. Her studies investigated the implications of KatG's highly oxidizable structure.  KatG contains an inordinate number of tryptophan residues (~4 times that observed in the typical enzyme). Its high content of Trp as well as other oxidizable side chains (Tyr and Met) supports a novel peroxidatic function that synergistically supports the enzyme's robust catalase activity.  Indeed, KatG's substantial catalase activity has arisen because of the novel covalent adduct that joins a Met, Tyr, and Trp side chain to create an entirely unique protein-based cofactor.  Jessica successfully defended her dissertation on September 3, 2021. It is entitled: Impact of the Highly Oxidizable Scaffold of Catalase-Peroxidase (KatG): Modulation of a Heme Peroxidase for Catalytic Versatility.  After receiving her PhD here at Auburn, Jessica moved to a postdoctoral position in the laboratory of Karen Anderson at Yale University School of Medicine. 

Publications and Abstracts
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., Martins, F. 2021. Designing new antitubercular isoniazid derivatives with improved reactivity and membrane trafficking abilities. Pharmacol. Res. 144, 112362.

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

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

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.

Minton, L. E., Xu, H., Krewall, J. R., Barton, C. M., and Goodwin, D. C. 2020. Impact of heme incorporation procedure on intermediates of KatG reaction with peroxides. 52nd Southeastern Undergraduate Research Conference, Tuscaloosa, AL, January 25, 2020.

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

Krewall, J. R., Sahrmann, P. G., and Goodwin, D. C. 2019. 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.

Aziz, T., Barton, C. M., Krewall, J. R., Xu, H., and Goodwin, D. C. 2019. “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.

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

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

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.

 Krewall, J. R., Njuma, O. J., and Goodwin, D. C. 2017. Role reversal between peroxidase reaction intermediates generates the distinct catalase mechanism of catalase-peroxidase. 46th Annual Southeast Magnetic Resonance Conference, Tallahassee, FL, (10/29/17).

Xu, H., Krewall, J. R., Njuma, O. J., and Goodwin, D. C. 2017. How an arginine switch preserves the catalase activity of KatG: Strategic use of an active-site tryptophan for off-pathway electron transfer. 46th Annual Southeast Magnetic Resonance Conference, Tallahassee, FL, (10/29/17).

Xu, H., Krewall, J. R., Njuma, O. J., Davis, I., Liu, A., and Goodwin, D. C. 2017. 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, (7/16/17 – 7/21/17).

Krewall, J. R., Xu, H., Njuma, O. J., and Goodwin, D. C. 2017. Directing off-pathway protein oxidation to preserve enzyme activity: At last, a role for the proximal tryptophan of KatG. 8th Annual Southeast Enzyme Conference, Atlanta, GA, (04/08/17).

Xu, H., Krewall, J. R., Njuma, O. J., and Goodwin, D. C. 2017. How an arginine switch preserves the catalase activity of KatG: Strategic use of an active-site tryptophan for off-pathway electron transfer. 8th Annual Southeast Enzyme Conference, Atlanta, GA, (04/08/17).