doi: 10.1038/373580a0.
Crystal structure of the nickel-iron hydrogenase from Desulfovibrio gigas
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- PMID: 7854413
- DOI: 10.1038/373580a0
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Crystal structure of the nickel-iron hydrogenase from Desulfovibrio gigas
Nature.
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Abstract
The X-ray structure of the heterodimeric Ni-Fe hydrogenase from Desulfovibrio gigas, the enzyme responsible for the metabolism of molecular hydrogen, has been solved at 2.85 A resolution. The active site, which appears to contain, besides nickel, a second metal ion, is buried in the 60K subunit. The 28K subunit, which coordinates one [3Fe-4S] and two [4Fe-4S] clusters, contains an amino-terminal domain with similarities to the redox protein flavodoxin. The structure suggests plausible electron and proton transfer pathways.
Comment in
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Redox enzymes. Splitting molecular hydrogen.Nature. 1995 Feb 16;373(6515):556-7. doi: 10.1038/373556a0. Nature. 1995. PMID: 7854404 No abstract available.
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