1FRV

CRYSTAL STRUCTURE OF THE OXIDIZED FORM OF NI-FE HYDROGENASE

Summary for 1FRV

• Entry DOI: 10.2210/pdb1frv/pdb
• Descriptor: HYDROGENASE, IRON/SULFUR CLUSTER, FE3-S4 CLUSTER, ... (6 entities in total)
• Functional Keywords: ni-fe hydrogenase, oxidoreductase
• Biological source: Desulfovibrio gigas; More
• Cellular location: Periplasm: P12943 P12944
• Total number of polymer chains: 4
• Total formula weight: 178832.70

Authors

Volbeda, A.,Frey, M.,Fontecilla-Camps, J.C. (deposition date: 1996-03-28, release date: 1996-11-08, Last modification date: 2024-10-23)

Primary citation

Volbeda, A.,Charon, M.H.,Piras, C.,Hatchikian, E.C.,Frey, M.,Fontecilla-Camps, J.C.
Crystal structure of the nickel-iron hydrogenase from Desulfovibrio gigas.
Nature, 373:580-587, 1995

PubMed 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.

PubMed: 7854413
DOI: 10.1038/373580a0

Experimental method

X-RAY DIFFRACTION (2.85 Å)