Native and mutant nickel-iron hydrogenases:: Unravelling structure and function

被引：46

作者：

de Lacey, AL

Fernández, VM

Rousset, M

机构：

[1] CSIC, Inst Catalisis, Madrid 28049, Spain

[2] CNRS, Unite Bioenerget & Ingn Prot, Inst Biol Struct & Microbiol, F-13402 Marseille, France

来源：

COORDINATION CHEMISTRY REVIEWS | 2005年 / 249卷 / 15-16期

关键词：

NiFe] hydrogenase; nickel; iron; EPR; FrIR; H-2; biocatalysis; DFT;

D O I：

10.1016/j.ccr.2005.03.009

中图分类号：

O61 [无机化学];

学科分类号：

070301 ; 081704 ;

摘要：

In this review, an appraisal of the progress in understanding of the NiFe-hydrogenases catalytic mechanism is presented. The article is focussed on NiFe-hydrogenases from Desulfovibrio genus, as these are among the best-characterized H-2-splitting enzymes. The X-ray structures, catalytic reactivity, spectroscopic properties and computer modeling data of the different forms of this class of hydrogenase are analyzed. In addition, the contribution of site-directed mutagenesis studies of Desulfovibrio fructosovorans species to structure-function relationships is reviewed. (c) 2005 Elsevier B.V. All rights reserved.

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页码：1596 / 1608

页数：13

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