Mark J. Snider

Degrees

B.A. Capital University, Chemistry 1997
Ph.D. University of North Carolina at Chapel Hill, Biochemistry & Biophysics 2001

Areas of Interest

Mechanistic and structural enzymology of bacterial degradation of nicotinic acid.
Using stopped-flow spectrophotometry to investigate kinetic mechanisms of flavin monooxygenases.
Functional characterization of novel phosphagen kinases, with the goal of discerning the evolution of substrate specificity, cooperative substrate binding and quaternary structure.

Courses Taught

Independent Study Advising

Takoda Zuehlke (2023) BCMB: Identification of a putative binding mechanism for the reducing substrate of 6-hydroxynicotinate 3-monooxygenase
May Z. Hlaing(2022) BCMB: Investigating substrate specificity for 6-hydroxynicotinate-3-monooxygenase (NicC) with alternative substrates: consequences to catalysis of replacing or removing the ring nitrogen
Robert Beal (2022) BCMB: Role of tight binding in negative cooperativity in the dimeric mitochondrial taurocyamine kinase from Arenicola brasiliensis

Publications

Z. R. Turlington; S. V. Ferreira de Macedo; K. Perry; S. L. Belsky*; J. A. Faust; M. J. Snider, K. A. Hicks (2023) Ligand bound structure of a 6‐hydroxynicotinic acid 3‐monooxygenase provides mechanistic insights; Accepted for publication in Archives in Biochemistry & Biophysics
S. W. Perkins*, M. Z. Hlaing*, K. A. Hicks, L. Rajakovich, M. J. Snider (2023) Mechanism of the multi-step catalytic cycle of 6-hydroxynicotinate 3-monooxygenase revealed by global kinetic analysis; Biochemistry 62; 1553-1567.
P. Piper*, B. Begres*, M. Snider, D. Fraga (2020) Two cryptosporidia species encode active creatine kinases that are not seen in other Apicomplexa species; Comparative Biochemistry and Physiology – Part B 246, 110459.
K. D. Nakamoto*, S. W. Perkins*, R. G. Campbell*, M. R. Bauerle*, T. G. Gerwig*, S. Gerislioglu, C. Wesdemiotis, M. A. Anderson, K. A. Hicks, M. J. Snider (2019) Mechanism of 6-hydroxynicotinate 3-monoxygenase, a flavin-dependent decarboxylative hydroxylase involved in aerobic nicotinic acid degradation. Biochemistry 58; 1751-1763.
K. A. Hicks, M. E. Yuen, W.- F. Zhen, T. J. Gerwig*, R. W. Story*, M. Kopp, M. J. Snider (2016) Structural and biochemical characterization of 6-hydroxynicotinic acid 3-monooxygenase, a novel decarboxylative hydroxylase involved in aerobic nicotinate degradation. Biochemistry 55, 3432–3446.

Presentations

Mark J. Snider and Katherine A. Hicks (2024) Novel enzymology of nicotinic acid degradation in Bacillus niacini. 28th Enzyme Mechanism Conference, Naples, FL, January 2024.
Mark J. Snider, Jack Redick, May Hlaing and Lauren Rajakovich (2023) Probing substrate specificity in the class A flavin enzyme 6-hydroxynicotinate 3-monooxygenase; Midwest Enzyme Chemistry Conference, Northwestern University, Evanston, IL, September 2023

Awards

National Science Foundation (2018-present), Molecular Biophysics Program RUI: Collaborative Research: Enzymology of Bacterial Nicotinic Acid Catabolism by Mark Snider (PI), Katherine Hicks (PI, SUNY Cortland) $ 551,536.
National Science Foundation (2016-2019), Major Research Instrumentation Program Acquisition of an NMR Spectrometer to Sustain Excellence in Undergraduate Research with Paul Bonvallet (PI), Judith Amburgey-Peters, Spring Knapp and Sarah Sobeck
Research Corporation for Science Advancement: Multi-Investigator Cottrell College Science Award Program (2012-2014), “Bacterial Degradation of Pharmaceuticals and Personal Care Products During Waste Water Treatment” with Stephanie Strand (Biology) and Melissa Schultz (Chemistry).
National Science Foundation (2008-2011), “Acquisition of an LC/MS/MS to Enhance Undergraduate Research and Teaching” with Melissa Schultz and Paul Edmiston (Chemistry).
National Science Foundation (2006-2009), “Acquisition of an Isothermal Titration Calorimeter” with Paul Bonvallet (Chemistry) and Don Jacobs (Physics).
National Science Foundation (2004-2007), “RUI: Comparative Structure – Function Analysis of Phosphagen Kinases” with Paul Edmiston and Dean Fraga (Biology).