Redox properties of the iron-sulfur clusters in activated Fe-hydrogenase from Desulfovibrio vulgaris (Hildenborough)

Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/65750/1/j.1432-1033.1992.tb17261.x.pd

COMPARISON OF THE NH2-TERMINAL AMINO-ACID SEQUENCES OF THE 4 NON-IDENTICAL SUBUNITS OF THE NAD-LINKED HYDROGENASES FROM NOCARDIA-OPACA 1B AND ALCALIGENES-EUTROPHUS H16

ZABOROSCH C, Schneider K, SCHLEGEL HG, KRATZIN H. COMPARISON OF THE NH2-TERMINAL AMINO-ACID SEQUENCES OF THE 4 NON-IDENTICAL SUBUNITS OF THE NAD-LINKED HYDROGENASES FROM NOCARDIA-OPACA 1B AND ALCALIGENES-EUTROPHUS H16. EUROPEAN JOURNAL OF BIOCHEMISTRY. 1989;181(1):175-180

Evidence for selenocysteine coordination to the active site nickel in the [NiFeSe]hydrogenases from Desulfovibrio baculatus.

Ni and Se x-ray absorption spectroscopic studies of the [NiFeSe]hydrogenases from Desulfovibrio baculatus are described. The Ni site geometry is pseudo-octahedral with a coordinating ligand composition of 3-4 (N,O) at 2.06 A, 1-2 (S,Cl) at 2.17 A, and 1 Se at 2.44 A. The Se coordination environment consists of 1 C at 2.0 A and a heavy scatterer M (M = Ni or Fe) at approximately 2.4 A. These results are interpreted in terms of a selenocysteine residue coordinated to the Ni site. The possible role of the Ni-Se site in the catalytic activation of H2 is discussed