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.
Laboratoire de Cristallographie et de Cristallogénèse des Protéines, Institut de Biologie Structurale J. P. Ebel (CEA, CNRS), Grenoble, France.
A
A
Volbeda
M H
MH
Charon
C
C
Piras
E C
EC
Hatchikian
M
M
Frey
J C
JC
Fontecilla-Camps
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