Journal
JOURNAL OF BIOCHEMISTRY
Volume 160, Issue 5, Pages 251-258Publisher
OXFORD UNIV PRESS
DOI: 10.1093/jb/mvw048
Keywords
hydrogenase; [NiFe] active site; oxygen tolerance; X-ray crystallography; [4Fe-3S] cluster
Categories
Funding
- Max Planck Society
- JST (CREST)
- JSPS [25291038, 24657077]
- Mitsubishi Foundation
- ENEOS Hydrogen Trust
- Grants-in-Aid for Scientific Research [24657077] Funding Source: KAKEN
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Hydrogenases catalyze the reversible conversion of molecular hydrogen to protons and electrons via a heterolytic splitting mechanism. The active sites of [NiFe] hydrogenases comprise a dinuclear Ni-Fe center carrying CO and CN- ligands. The catalytic activity of the standard (O-2-sensitive) [NiFe] hydrogenases vanishes under aerobic conditions. The O-2-tolerant [NiFe] hydrogenases can sustain H-2 oxidation activity under atmospheric conditions. These hydrogenases have very similar active site structures that change the ligand sphere during the activation/catalytic process. An important structural difference between these hydrogenases has been found for the proximal iron-sulphur cluster located in the vicinity of the active site. This unprecedented [4Fe-3S]-6Cys cluster can supply two electrons, which lead to rapid recovery of the O-2 inactivation, to the [NiFe] active site.
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