Jarett Wilcoxen

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B.S. in Biochemistry, University of California, Santa Barbara (2007)

Ph.D. in Biochemistry and Molecular Biology, University of California, Riverside (2013)

Research Advisor: Prof. Russ Hille

Thesis Title: Kinetic, Mechanistic, and Spectroscopic Studies of the Mo- and Cu- Containing CO dehydrogenase from Oligotropha carboxidovorans


Publications: (* Denotes equal contribution)

Rettberg, L.A.*, Wilcoxen, J.*,Lee, C.C., Stiebritz, M.T., Tanifuji, K., Britt, R.D., and Hu, Y.
Probing the Coordination and Function of Fe4S4 Modules in Nitrogenase Assembly Protein NifB
Nature Communications, 2018, 9, Article number: 2824 doi:10.1038/s41467-018-05272-8

Lee, C.C., Wilcoxen, J., Hiller, C.J., Britt, R.D. and Hu, Y. Evaluation of the Catalytic Relevance of the CO-bound States of V-Nitrogenase. Angew. Chem. Int. Ed. 2018, 57, 3411–3414 dx.doi.org/10.1002/anie.201800189 

Wilcoxen, J., Bruender, N.A., Bandarian, V., Britt, R.D. A Radical Intermediate is identified in QueE from Bacillus subtilisusing 6-Carboxypterin as an alternative substrate. JAm. Chem. Soc. 2018, 140, 1753–1759 dx.doi.org/10.1021/jacs.7b10860

Pearl, N.M., Wilcoxen, J., Im, S., Kunz, R., Darty, J., Britt, R.D., Ragsdale, S.W., Waskell, L. Protonation of the Hydroperoxo Intermediate of Cytochrome P450 2B4 is Slower in the Presence of Cytochrome P450 Reductase than in the Presence of Cytochrome b5Biochemistry2016, 55, 6558–6567 dx.doi.org/10.1021/acs.biochem.6b00996

Dingwall, S., Wilcoxen, J., Niks, D., Hille, R. Studies of carbon monoxide dehydrogenase from Oligotropha carboxidovoransJournal of Molecular Catalysis B: Enzymatic2016, 134, 317-322 dx.doi.org/10.1016/j.molcatb.2016.10.007

Wilcoxen, J.*, Arragain, S.*, Scandurra, A.A., Jimenez-Vicente, E., Echavarri-Erasun, C., Pollmann, S., Britt, R.D., and Rubio, L.M. Electron Paramagnetic Resonance Characterization of Three Iron–Sulfur Clusters Present in the Nitrogenase Cofactor Maturase NifB from Methanocaldococcus infernus. JAm. Chem. Soc2016, 138, 7468-7471 dx.doi.org/10.1021/jacs.6b03329

Bruender, N.A., Wilcoxen, J., Britt, R.D., and Bandarian, V. Biochemical and spectroscopic characterization of a radical SAM enzyme involved in the formation of a peptide thioether crosslink. Biochemistry. 2016, 55, 2122-2134 dx.doi.org/10.1021/acs.biochem.6b00145

Zhu, W.*, Wilcoxen, J.*, Britt, R.D., and Richards, N.G.J. Formation of Hexacoordinate Mn(III) in Bacillus subtilis Oxalate Decarboxylase Requires Catalytic Turnover. Biochemistry. 2016, 55, 429-434 dx.doi.org/10.1021/acs.biochem.5b01340 

Hille, R., Dingwall, S., Wilcoxen, J. The aerobic CO dehydrogenase from Oligotropha carboxidovorans. Bio. Inorg. Chem. 2015 20, 243-251 dx.doi.org/10.1007/s00775-014-1188-4

Shanmugam, M., Wilcoxen, J., Kirk, M., Hoffman, B., and Hille, R. 13C and 63,65Cu ENDOR studies of CO dehydrogenase from Oligotropha carboxidovorans. Experimental evidence in support of a copper-carbonyl intermediate. J. Am. Chem. Soc2013, 135, 17775 dx.doi.org/10.1021/ja406136f

Wilcoxen, J. and Hille, R. Kinetic and Spectroscopic Studies of H2Oxidation by the Mo/Cu containing Carbon Monoxide Dehydrogenase of Oligotropha carboxidovorans. J. Biol. Chem. 2013, 288, 36052-36060 dx.doi.org/10.1074/jbc.M113.522441

Hille, R., Wilcoxen, J., Zhang, B., and Snider, S. CO Dehydrogenase from Oligotropha carboxidovorans Flavins and Flavoproteins 2011; 1 ed., Lulu, Raleigh, NC, 2013 ISBN-13: 978-1300786405

Wilcoxen, J.; Hille, R.; Zhang, B. The Reaction of the Molybdenum- and Copper- Containing Carbon Monoxide Dehydrogenase from Oligotropha carboxydovoranswith Quinones Flavins and Flavoproteins 2011; 1 ed.; Lulu: Raleigh, NC, 2013 ISBN-13: 978-1300786405

Wilcoxen, J., Snider, S., and Hille, R. Substitution of Silver for Copper in the Binuclear Mo/Cu Center of Carbon Monoxide Dehydrogenase from Oligotropha carboxidovoransJ. Am. Chem. Soc. 2011 133, 12934-12936 dx.doi.org/10.1021/ja205073j

Wilcoxen J.,Zhang, B., and Hille, R. Reaction of the Molybdenum- and Copper-Containing Carbon Monoxide Dehydrogenase from Oligotropha carboxydovoranswith Quinones. Biochemistry. 2011 50, 1910–1916 dx.doi.org/10.1021/bi1017182