Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 142, Issue 3, Pages 1227-1235Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jacs.9b08756
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Funding
- Biological and Electron Transfer and Catalysis (BETCy) EFRC, an Energy Frontier Research Center - U.S. Department of Energy, Office of Science [DE-SC0012518]
- U.S. Department of Energy (DOE) [DE-AC36-08GO28308]
- U.S. Department of Energy, Office of Science, Office of Basic Energy Sciences [DE-AC02-76SF00515]
- U.S. Department of Energy Office of Biological and Environmental Research
- National Institutes of Health (NIH), National Institute of General Medical Sciences [P41GM103393]
- Center for Molecular Electrocatalysis (CME), an Energy Frontier Research Center - U.S. DOE, Office of Science, Office of Basic Energy Sciences (BES)
- U.S. DOE, Office of Science, BES, Division of Chemical Sciences, Geosciences, and Bio-Sciences [DE-AC05-76RL01830]
- Department of Energy's Office of Biological and Environmental Research at Pacific Northwest National Laboratory
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Hydrogenases display 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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