Victor L. Davidson

Affiliations: 
The University of Mississippi Medical Center, Jackson, MS, United States 
Area:
Biochemistry
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"Victor Davidson"
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Publications

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Mamounis KJ, Yukl ET, Davidson VL. (2020) Roles of active site residues in catalysis, substrate binding, cooperativity and the reaction mechanism of the quinoprotein glycine oxidase. The Journal of Biological Chemistry
Ma Z, Abendroth J, Buchko GW, et al. (2020) Crystal structure of a hemerythrin-like protein from Mycobacterium kansasii and homology model of the orthologous Rv2633c protein of M. tuberculosis. The Biochemical Journal
Mamounis KJ, Avalos D, Yukl ET, et al. (2019) Kinetic and structural evidence that Asp-678 plays multiple roles in catalysis by the quinoprotein glycine oxidase. The Journal of Biological Chemistry
Mamounis KJ, Ma Z, Sanchez-Amat A, et al. (2019) Characterization of PlGoxB, a flavoprotein required for cysteine tryptophylquinone biosynthesis in glycine oxidase from Pseudoalteromonas luteoviolacea. Archives of Biochemistry and Biophysics. 108110
Ma Z, Davidson VL. (2019) Redox properties of a cysteine tryptophylquinone-dependent glycine oxidase are distinct from those of tryptophylquinone-dependent dehydrogenases. Biochemistry
Avalos D, Sabuncu S, Mamounis KJ, et al. (2019) Structural and spectroscopic characterization of a product Schiff-base intermediate in the reaction of the quinoprotein glycine oxidase, GoxA. Biochemistry
Yukl ET, Davidson VL. (2018) Diversity of structures, catalytic mechanisms and processes of cofactor biosynthesis of tryptophylquinone-bearing enzymes. Archives of Biochemistry and Biophysics. 654: 40-46
Davidson VL. (2018) Protein-derived Cofactors Revisited: Empowering Amino Acid Residues with New Functions. Biochemistry
Andreo-Vidal A, Mamounis K, Sehanobish E, et al. (2018) Structure and enzymatic properties of an unusual cysteine tryptophylquinone-dependent glycine oxidase from Pseudoalteromonas luteoviolacea. Biochemistry
Ma Z, Strickland KT, Cherne MD, et al. (2017) The Rv2633c protein of Mycobacterium tuberculosis is a non-heme di-iron catalase with a possible role in defenses against oxidative stress. The Journal of Biological Chemistry
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