Journal
ELECTROCHIMICA ACTA
Volume 199, Issue -, Pages 349-356Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.electacta.2016.02.119
Keywords
electron-transfer; voltammetry; CO2; ferredoxin
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Funding
- Research Corporation for Science Advancement
- Department of Energy Office of Science [DE-SC0012598]
- U.S. Department of Energy (DOE) [DE-SC0012598] Funding Source: U.S. Department of Energy (DOE)
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Enzymes from the 2-oxoacid: ferredoxin oxidoreductase (OFOR) family engage in both CO2 evolution and reduction in nature, depending on their physiological roles. Two enzymes and their redox partner ferredoxins (Fds) from Hydrogenobacter thermophilus and Desulfovibrio africanus were examined to investigate the basis of the catalytic bias. The Fd1 from H. thermophilus demonstrated a potential of similar to -485 mV at room temperature, the lowest for known single [4Fe-4S] cluster Fds. It suggests a low potential electron donor may be the key factor in overcoming the large thermodynamic barrier of CO2 reduction. The Fd-mediated electrocatalytic experiments further demonstrated the impact of Fd's potential on the direction of the OFOR reaction: as OFOR enzymes could essentially catalyze both CO2 evolution and reduction in vitro, the difference in their physiological roles is associated with the reduction potential of the redox partner Fd. The electrocatalytic assay could study both CO2 evolution and reduction in one setup and is a good tool to probe Fds' reactivity that arise from their reduction potentials. (C) 2016 Elsevier Ltd. All rights reserved.
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