来自杆状脱硫弧菌的[NiFeSe]氢化酶中硒代半胱氨酸与活性位点镍配位的证据。
Evidence for selenocysteine coordination to the active site nickel in the [NiFeSe]hydrogenases from Desulfovibrio baculatus.
作者信息
Eidsness M K, Scott R A, Prickril B C, DerVartanian D V, Legall J, Moura I, Moura J J, Peck H D
机构信息
Department of Chemistry, University of Georgia, Athens 30602.
出版信息
Proc Natl Acad Sci U S A. 1989 Jan;86(1):147-51. doi: 10.1073/pnas.86.1.147.
Abstract
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.
摘要
描述了对来自杆状脱硫弧菌的[NiFeSe]氢化酶的镍和硒X射线吸收光谱研究。镍位点的几何形状为伪八面体，配位配体组成如下：在2.06埃处有3 - 4个（N，O）原子，在2.17埃处有1 - 2个（S，Cl）原子，在2.44埃处有1个硒原子。硒的配位环境由在2.0埃处的1个碳原子和在约2.4埃处的一个重散射体M（M = Ni或Fe）组成。这些结果被解释为一个硒代半胱氨酸残基与镍位点配位。讨论了Ni - Se位点在H2催化活化中的可能作用。
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