Journal
ACS CATALYSIS
Volume 7, Issue 3, Pages 2145-2150Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acscatal.6b03276
Keywords
[FeFe]-hydrogenase; kinetics; enzymology; electron bifurcation; time-resolved infrared spectroscopy
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Funding
- Biological Electron Transfer and Catalysis Energy Frontier Research Center-U.S. Department of Energy, Office of Science, Basic Energy Sciences [DE-SC0012518]
- National Science Foundation [DMR1409851]
- Division Of Materials Research
- Direct For Mathematical & Physical Scien [1409851] Funding Source: National Science Foundation
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[FeFd]-hydrogenases catalyze the reversible production of hydrogen gas from protons and electrons, but the mechanism of catalysis is still the subject of debate. In this report, we describe a pre-steady-state photoreduction methodology for correlating putative intermediates to the reactivity of an [FeFe]-hydrogenase from Thermotoga maritima. In this method, MV+ is rapidly formed photochemically by pulsed laser excitation and the intermolecular ET and active site dynamics are followed by nanosecond time-resolved visible and infrared spectroscopy, respectively. The results kinetically validate the H-ox H-red and H-sred intermediates, strongly supporting a vast body of literature on their involvement in proton reduction.
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