Crystal structure of the nickel-iron hydrogenase from Desulfovibrio gigas.
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.
Volbeda
A
A
Laboratoire de Cristallographie et de Cristallogénèse des Protéines, Institut de Biologie Structurale J. P. Ebel (CEA, CNRS), Grenoble, France.
Charon
M H
MH
Piras
C
C
Hatchikian
E C
EC
Frey
M
M
Fontecilla-Camps
J C
JC
D000595:Amino Acid Sequence; D001665:Binding Sites; D003196:Computer Graphics; D018360:Crystallography, X-Ray; D003901:Desulfovibrio / Q000201:enzymology*; D004579:Electron Transport; D006864:Hydrogenase / Q000737:chemistry* / Q000378:metabolism; D007501:Iron / Q000737:chemistry*; D007506:Iron-Sulfur Proteins / Q000737:chemistry; D008969:Molecular Sequence Data; D009532:Nickel / Q000737:chemistry*; D011487:Protein Conformation; D011499:Protein Processing, Post-Translational; D011522:Protons
D007506:Iron-Sulfur Proteins; D011522:Protons; D009532:Nickel; D007501:Iron; C043296:nickel-iron hydrogenase; D006864:Hydrogenase