Crystal structure of the nickel-iron hydrogenase f...[Nature. 1995] - PubMed Result

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1: Nature. 1995 Feb 16;373(6515):580-7. Links

Comment in:: Nature. 1995 Feb 16;373(6515):556-7.

Crystal structure of the nickel-iron hydrogenase from Desulfovibrio gigas.

Volbeda A, Charon MH, Piras C, Hatchikian EC, Frey M, Fontecilla-Camps JC.

Laboratoire de Cristallographie et de Cristallogénèse des Protéines, Institut de Biologie Structurale J. P. Ebel (CEA, CNRS), Grenoble, France.

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.

PMID: 7854413 [PubMed - indexed for MEDLINE]

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Structures reported by this article

Structure Of The Unready Oxidized Form Of [nife] Hydrogenase

PDB: 1YQ9

Source: Desulfovibrio gigas

Method: X-Ray Diffraction | Resolution: 2.35 Å
» See all 2 structures...

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Crystal structure of the nickel-iron hydrogenase from Desulfovibrio gigas.Crystal structure of the nickel-iron hydrogenase from Desulfovibrio gigas.

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