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Proc Natl Acad Sci U S A. 2012 Jul 17;109(29):11516-21. doi: 10.1073/pnas.1204770109. Epub 2012 Jul 16.

Electrocatalytic mechanism of reversible hydrogen cycling by enzymes and distinctions between the major classes of hydrogenases.

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1
Inorganic Chemistry Laboratory, Department of Chemistry, University of Oxford, South Parks Road, Oxford OX1 3QR, United Kingdom.

Erratum in

  • Proc Natl Acad Sci U S A. 2012 Oct 30;109(44):18232-3.

Abstract

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.

PMID:
22802675
PMCID:
PMC3406873
DOI:
10.1073/pnas.1204770109
[Indexed for MEDLINE]
Free PMC Article
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