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Electrocatalytic mechanism of reversible hydrogen cycling by enzymes and distinctions between the major classes of hydrogenases
Open accessAbstract
The extraordinary ability of Fe- and Ni-containing enzymes to catalyze rapid and efficient H + /H 2 interconversion—a property otherwise exclusive to platinum metals—has been investigated in a series of experiments combining variable-temperature protein film voltammetry with mathematical modeling. The results highlight important differences between the catalytic performance of [FeFe]-hydrogenases and [NiFe]-hydrogenases and justify a simple model for reversible catalytic electron flow in enzymes and electrocatalysts that should be widely applicable in fields as diverse as electrochemistry, catalysis, and bioenergetics. The active site of [FeFe]-hydrogenases, an intricate Fe-carbonyl complex known as the “H cluster,” emerges as a supreme catalyst.
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Cited by
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Can, M., Armstrong, F. A., & Ragsdale, S. W. (2014) · Chemical Reviews · doi:10.1021/cr400461p · Cited by 622
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Metadata
- Authors
- Hexter, S. V., Grey, F., Happe, T., Climent, V., & Armstrong, F. A.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2012-07-12
- Volume
- 109
- Issue
- 29
- Pages
- 11516-11521
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2151091298
- Cited by
- 174
- References
- 0
- FWCI
- 4.25
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Hexter, S. V., Grey, F., Happe, T., Climent, V., & Armstrong, F. A. (2012). Electrocatalytic mechanism of reversible hydrogen cycling by enzymes and distinctions between the major classes of hydrogenases. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.1204770109
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