Structural mimics for the active site of [NiFe] hydrogenase

被引：140

作者：

Marr, AC ^{[1
]}

Spencer, DJE ^{[1
]}

Schröder, M ^{[1
]}

机构：

[1] Univ Nottingham, Sch Chem, Nottingham NG7 2RD, England

来源：

COORDINATION CHEMISTRY REVIEWS | 2001年 / 219卷

关键词：

NiFe] hydrogenase; modelling; nickel; iron; thiolate; synthesis; bioinorganic;

D O I：

10.1016/S0010-8545(01)00396-4

中图分类号：

O61 [无机化学];

学科分类号：

070301 ; 081704 ;

摘要：

Hydrogenases are enzymes that catalyse the reversible two-electron oxidation of H-2. The [NiFe] hydrogenases have been characterised spectroscopically and by single crystal X-ray diffraction, and show an active site incorporating a heterobinuclear [NiFe] centre bridged by two cysteine S-donors. Low molecular weight synthetic complex models, which structurally mimic the dithiolate-bridged [NiFe] centre, serve as important probes of structure and chemistry at the active site and are the subject of this review. (C) 2001 Elsevier Science B.V. All rights reserved.

引用

页码：1055 / 1074

页数：20

共 90 条

[41] Electronic structure of linear thiophenolate-bridged heterotrinuclear complexes [LFeMFeL]n+ (M = Cr, Co, Fe; n = 1-3):: Localized vs delocalized models [J].