1frv

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1frv, resolution 2.85Å

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CRYSTAL STRUCTURE OF THE OXIDIZED FORM OF NI-FE HYDROGENASE

Overview

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.

About this Structure

1FRV is a Protein complex structure of sequences from Desulfovibrio gigas with NI, SF4, F3S and FEL as ligands. Active as Cytochrome-c3 hydrogenase, with EC number 1.12.2.1 Full crystallographic information is available from OCA.

Reference

Crystal structure of the nickel-iron hydrogenase from Desulfovibrio gigas., Volbeda A, Charon MH, Piras C, Hatchikian EC, Frey M, Fontecilla-Camps JC, Nature. 1995 Feb 16;373(6515):580-7. PMID:7854413

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