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

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

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

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

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

Redox enzymes. Splitting molecular hydrogen. [Nature. 1995]
Redox enzymes. Splitting molecular hydrogen.Cammack R. Nature. 1995 Feb 16; 373(6515):556-7.

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Cited by 92 PubMed Central articles

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

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