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

Marly K. Eidsness | Zendy; Robert A. Scott | Zendy; B C Prickril | Zendy; D.V. Dervartanian | Zendy; Jean LeGall | Zendy; Isabel Moura | Zendy; José J. G. Moura | Zendy; H.D. Peck | Zendy

Open Access

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

Author(s) -

Marly K. Eidsness,

Robert A. Scott,

B C Prickril,

D.V. Dervartanian,

Jean LeGall,

Isabel Moura,

José J. G. Moura,

H.D. Peck

Publication year - 1989

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.86.1.147

Subject(s) - selenocysteine , hydrogenase , octahedron , active site , nickel , chemistry , ligand (biochemistry) , coordination complex , crystallography , catalysis , stereochemistry , cysteine , metal , biochemistry , crystal structure , enzyme , organic chemistry , receptor

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.

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