Kevin R. Hoke, PhD

Affiliations: 
Berry College, Rome, GA, United States 
Area:
metalloprotein electrochemistry
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"Kevin Hoke"
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Publications

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Deng Y, Weaver ML, Hoke KR, et al. (2019) A Heme Propionate Staples the Structure of Cytochrome for Methionine Ligation to the Heme Iron. Inorganic Chemistry
Deng Y, Zhong F, Alden S, et al. (2018) The K79G Mutation Reshapes the Heme Crevice and Alters Redox Properties of Cytochrome c. Biochemistry
Amacher JF, Zhong F, Lisi GP, et al. (2018) Correction to "A Compact Structure of Cytochrome c Trapped in a Lysine-Ligated State: Loop Refolding and Functional Implications of a Conformational Switch". Journal of the American Chemical Society
Amacher JF, Zhong F, Lisi GP, et al. (2015) A Compact Structure of Cytochrome c Trapped in a Lysine-Ligated State: Loop Refolding and Functional Implications of a Conformational Switch. Journal of the American Chemical Society
Breton GW, Hoke KR. (2013) Application of radical cation spin density maps toward the prediction of photochemical reactivity between N-methyl-1,2,4-triazoline-3,5-dione and substituted benzenes. The Journal of Organic Chemistry. 78: 4697-707
Fourmond V, Hoke K, Heering HA, et al. (2009) SOAS: a free program to analyze electrochemical data and other one-dimensional signals. Bioelectrochemistry (Amsterdam, Netherlands). 76: 141-7
Hoke KR, Crane BR. (2009) The solution electrochemistry of tetrahydrobiopterin revisited. Nitric Oxide : Biology and Chemistry / Official Journal of the Nitric Oxide Society. 20: 79-87
Kang SA, Hoke KR, Crane BR. (2006) Solvent isotope effects on interfacial protein electron transfer in crystals and electrode films. Journal of the American Chemical Society. 128: 2346-55
Hoke KR, Cobb N, Armstrong FA, et al. (2004) Electrochemical studies of arsenite oxidase: an unusual example of a highly cooperative two-electron molybdenum center. Biochemistry. 43: 1667-74
Elliott SJ, Hoke KR, Heffron K, et al. (2004) Voltammetric studies of the catalytic mechanism of the respiratory nitrate reductase from Escherichia coli: how nitrate reduction and inhibition depend on the oxidation state of the active site. Biochemistry. 43: 799-807
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