Tuning Catalytic Bias of Hydrogen Gas Producing Hydrogenases
- 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.
- 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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