Research in the Hicks laboratory is focused on studying bacterial enzymes involved in interesting chemical transformations using a structure-function approach. We are particularly interested in metabolic enzymes due to their potential as drug targets and application to bioremediation efforts.
Along with Professor Mark Snider at the College of Wooster, our lab has received funding from the National Science Foundation for our work on the bacterial catabolism of nicotinic acid.
4. Kent D. Nakamoto*, Scott W. Perkins*, Selim Gerislioglu, Mark A. Anderson, Katherine A. Hicks, and Mark J. Snider. Mechanism of 6-hydroxynicotinate 3-monooxygenase, a flavin-dependent decarboxylative hydroxylase involved in aerobic nicotinic acid catabolism, Biochemistry, (2019) 58(13), 1751-1763.
3. Weijie Zhou, Andrew Tsai, Devon A. Dattmore, Devin P. Stives, Iva Chitrakar, Alexis Maria D’alessandro, Shiv Patel, Katherine A. Hicks, and Jarrod B. French. Crystal structure of E. coli PRPP synthetase, BMC Structural Biology, (2019), 19(1), 1-7.
2. Roger Shek, Devon A. Dattmore, Devin P. Stives, Ashley L. Jackson, Christa H. Chatfield, Katherine A. Hicks, and Jarrod B. French. “Structural and Functional Basis for Targeting Campylobacter jejuni Agmatine Deiminase To Overcome Antibiotic Resistance,” Biochemistry, (2017) 56 (51), 6734-6742.
1.Katherine A. Hicks, Meigan E. Yuen, Wei Feng Zhen, Tyler J. Gerwig*, Ryan W. Story*, Megan C. Kopp, and Mark J. Snider. “Structural and Biochemical Characterization of 6-Hydroxynicotinic Acid 3-Monooxygenase, a Novel Decarboxylative Hydroxylase Involved in Aerobic Nicotinate Degradation,” Biochemistry, (2016), 55(24), 3432-3446.
SUNY Cortland undergraduate author, The College of Wooster undergraduate author*