Crystal structure of the nickel-iron hydrogenase from Desulfovibrio gigas.

Title	Crystal structure of the nickel-iron hydrogenase from Desulfovibrio gigas.
Authors	A Volbeda, M Charon, C Piras, E C Hatchikian, M. Frey, J Fontecilla-Camps
Magazine	Nature
Date	02/16/1995
DOI	10.1038/373580a0
Introduction	The X-ray structure of the heterodimeric nickel-iron hydrogenase from Desulfovibrio gigas, an enzyme responsible for molecular hydrogen metabolism, was solved at 2.85 Å resolution. This enzyme's active site, containing nickel and a second metal ion, is located within the 60K subunit. The 28K subunit, containing [3Fe-4S] and [4Fe-4S] clusters, features an amino-terminal domain that shares a structural characteristic with the redox protein flavodoxin. The structure reveals potential pathways for electron and proton transfer, providing insights into the enzyme's function.
Quote	A Volbeda, M H Charon and C Piras et al. Crystal structure of the nickel-iron hydrogenase from Desulfovibrio gigas. Nature. 1995. DOI: 10.1038/373580a0
Element	Nickel (Ni) , Hydrogen (H)
Materials	Crystals
Industry	Research & Laboratory