Tuning Catalytic Bias of Hydrogen Gas Producing Hydrogenases

Artz, Jacob H.; Zadvornyy, Oleg A.; Mulder, David W.; Keable, Stephen M.; Cohen, Aina E.; Ratzloff, Michael W.; Williams, S. Garrett; Ginovska, Bojana; Kumar, Neeraj; Song, Jinhu; McPhillips, Scott E.; Davidson, Catherine M.; Lyubimov, Artem Y.; Pence, Natasha; Schut, Gerrit J.; Jones, Anne K.; Soltis, S. Michael; Adams, Michael W.  W.; Raugei, Simone; King, Paul W.; Peters, John W.

doi:10.1021/jacs.9b08756

Title: Tuning Catalytic Bias of Hydrogen Gas Producing Hydrogenases

Journal Article · 09 December 2019 · Journal of the American Chemical Society

DOI: https://doi.org/10.1021/jacs.9b08756 · OSTI ID:1593682

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Washington State Univ., Pullman, WA (United States); National Renewable Energy Lab. (NREL), Golden, CO (United States)
Washington State Univ., Pullman, WA (United States)
National Renewable Energy Lab. (NREL), Golden, CO (United States)
Montana State Univ., Bozeman, MT (United States)
SLAC National Accelerator Lab., Menlo Park, CA (United States). Stanford Synchrotron Radiation Lightsource (SSRL)
Arizona State Univ., Tempe, AZ (United States)
Pacific Northwest National Lab. (PNNL), Richland, WA (United States)
Univ. of Georgia, Athens, GA (United States)
Washington State Univ., Pullman, WA (United States); Pacific Northwest National Lab. (PNNL), Richland, WA (United States)
Washington State Univ., Pullman, WA (United States); Pacific Northwest National Lab. (PNNL), Richland, WA (United States); Montana State Univ., Bozeman, MT (United States)

Hydrogenases show a wide range of catalytic rates and biases in reversible hydrogen gas oxidation catalysis. The interactions of the iron-sulfur-containing catalytic site with the local protein environment are thought to contribute to differences in catalytic reactivity, but this has not been demonstrated. The microbe Clostridium pasteurianum produces three [FeFe]-hydrogenases that differ in 'catalytic bias' by exerting a disproportionate rate acceleration in one direction or the other that spans a remarkable 6 orders of magnitude. The combination of high-resolution structural work, biochemical analyses, and computational modeling indicates that protein secondary interactions directly influence the relative stabilization/destabilization of different oxidation states of the active site metal cluster. This selective stabilization or destabilization of oxidation states can preferentially promote hydrogen oxidation or proton reduction and represents a simple yet elegant model by which a protein catalytic site can confer catalytic bias.

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Research Organization:: Energy Frontier Research Centers (EFRC) (United States). Center for Biological Electron Transfer and Catalysis (BETCy). Center for Molecular Electrocatalysis (CME); National Renewable Energy Laboratory (NREL), Golden, CO (United States); Pacific Northwest National Laboratory (PNNL), Richland, WA (United States); SLAC National Accelerator Laboratory (SLAC), Menlo Park, CA (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES)

Grant/Contract Number:: AC36-08GO28308; AC05-76RL01830; AC02-76SF00515; SC0012518; P41GM103393

OSTI ID:: 1593682

Alternate ID(s):: OSTI ID: 1597671; OSTI ID: 1633991

Report Number(s):: NREL/JA-2700-74582; PNNL-SA-140081

Journal Information:: Journal of the American Chemical Society, Vol. 142, Issue 3; ISSN 0002-7863

Publisher:: American Chemical Society (ACS)Copyright Statement

Country of Publication:: United States

Language:: English

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