Hydrogenases: active site puzzles and progress

被引：167

作者：

Armstrong, FA ^{[1
]}

机构：

[1] Univ Oxford, Inorgan Chem Lab, Dept Chem, Oxford OX1 3QR, England

来源：

CURRENT OPINION IN CHEMICAL BIOLOGY | 2004年 / 8卷 / 02期

基金：

英国生物技术与生命科学研究理事会;

关键词：

D O I：

10.1016/j.cbpa.2004.02.004

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Recent research on the hydrogenase reactions has sought to probe beyond the information that is provided by X-ray diffraction structures. The major challenge of locating 'transient' hydrogen atoms in species that are potential catalytic intermediates is being addressed, using advanced electron paramagnetic resonance (EPR) techniques and theoretical methods. This article discusses recent progress towards a consensus on the structures of different states of the active site of hydrogenases, the mechanisms of activation and hydrogen cycling.

引用

页码：133 / 140

页数：8

共 46 条

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