Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
