Health & Environmental Research Online (HERO)


Print Feedback Export to File
1796965 
Journal Article 
Crystal structure of the nickel-iron hydrogenase from Desulfovibrio gigas 
Volbeda, A; Charon, MH; Piras, C; Hatchikian, EC; Frey, M; Fontecilla-Camps, JC 
1995 
1 
Nature
ISSN: 0028-0836
EISSN: 1476-4687 
373 
6515 
580-587 
English 
7854413 
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.