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1
Evidence for selenocysteine coordination to the active site nickel in the [NiFeSe]hydrogenases from Desulfovibrio baculatus.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。
Proc Natl Acad Sci U S A. 1989 Jan;86(1):147-51. doi: 10.1073/pnas.86.1.147.
2
EPR studies with 77Se-enriched (NiFeSe) hydrogenase of Desulfovibrio baculatus. Evidence for a selenium ligand to the active site nickel.用富含77Se的巴氏脱硫弧菌(NiFeSe)氢化酶进行的电子顺磁共振研究。活性位点镍存在硒配体的证据。
J Biol Chem. 1989 Feb 15;264(5):2678-82.
3
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4
The iron-sulfur centers of the soluble [NiFeSe] hydrogenase, from Desulfovibrio baculatus (DSM 1743). EPR and Mössbauer characterization.来自巴氏脱硫弧菌(DSM 1743)的可溶性[NiFeSe]氢化酶的铁硫中心。电子顺磁共振和穆斯堡尔谱表征。
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The direct role of selenocysteine in [NiFeSe] hydrogenase maturation and catalysis.硒代半胱氨酸在 [NiFeSe]氢化酶成熟和催化中的直接作用。
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The nickel site in active Desulfovibrio baculatus [NiFeSe] hydrogenase is diamagnetic. Multifield saturation magnetization measurement of the spin state of Ni(II).活性巴氏脱硫弧菌[NiFeSe]氢化酶中的镍位点是抗磁性的。对Ni(II)自旋态进行多场饱和磁化测量。
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8
The crystal structure of a reduced [NiFeSe] hydrogenase provides an image of the activated catalytic center.还原态[镍铁硒]氢化酶的晶体结构给出了活化催化中心的图像。
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Reactivity of [Fe] and [Ni-Fe-Se] hydrogenases with their oxido-reduction partner: the tetraheme cytochrome c3.[铁]氢化酶和[镍-铁-硒]氢化酶与其氧化还原伙伴:四血红素细胞色素c3的反应活性。
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本文引用的文献

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Desulfovibrio vulgaris hydrogenase: a nonheme iron enzyme lacking nickel that exhibits anomalous EPR and Mössbauer spectra.普通脱硫弧菌氢化酶:一种不含镍的非血红素铁酶,其电子顺磁共振(EPR)和穆斯堡尔谱显示异常。
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Desulfovibrio Gigas hydrogenase: redox properties of the nickel and iron-sulfur centers.巨大脱硫弧菌氢化酶:镍和铁硫中心的氧化还原特性
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Evidence for nickel and a three-iron center in the hydrogenase of Desulfovibrio desulfuricans.脱硫脱硫弧菌氢化酶中镍和三铁中心的证据。
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The presence of redox-sensitive nickel in the periplasmic hydrogenase from Desulfovibrio gigas.巨大脱硫弧菌周质氢化酶中氧化还原敏感镍的存在。
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A selenium-containing hydrogenase from Methanococcus vannielii. Identification of the selenium moiety as a selenocysteine residue.来自万氏甲烷球菌的一种含硒氢化酶。将硒部分鉴定为硒代半胱氨酸残基。
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10
A cytoplasmic nickel-iron hydrogenase with high specific activity from Desulfovibrio multispirans sp. N., a new species of sulfate reducing bacterium.来自多螺旋脱硫弧菌新种N.的一种具有高比活性的胞质镍铁氢化酶,该菌为一种硫酸盐还原细菌。
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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.

DOI:10.1073/pnas.86.1.147
PMID:2521386
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC286421/
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。