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氢化酶:活性位点谜题与进展

Hydrogenases: active site puzzles and progress.

作者信息

Armstrong Fraser A

机构信息

Department of Chemistry, University of Oxford, Inorganic Chemistry Laboratory, UK.

出版信息

Curr Opin Chem Biol. 2004 Apr;8(2):133-40. doi: 10.1016/j.cbpa.2004.02.004.

DOI:10.1016/j.cbpa.2004.02.004
PMID:15062773
Abstract

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.

摘要

最近关于氢化酶反应的研究试图探究超越X射线衍射结构所提供的信息。利用先进的电子顺磁共振(EPR)技术和理论方法,正在解决在潜在催化中间体物种中定位“瞬态”氢原子这一主要挑战。本文讨论了在氢化酶活性位点不同状态的结构、活化机制和氢循环方面达成共识的最新进展。

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