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工程化抗坏血酸过氧化物酶的活性位点。

Engineering the active site of ascorbate peroxidase.

作者信息

Lloyd Raven E, Celik A, Cullis P M, Sangar R, Sutcliffe M J

机构信息

Department of Chemistry, University of Leicester, University Road, Leicester, LE1 7RH, U.K.

出版信息

Biochem Soc Trans. 2001 May;29(Pt 2):105-11. doi: 10.1042/0300-5127:0290105.

Abstract

Understanding the catalytic versatility of haem enzymes, and in particular the relationships that exist between different classes of haem-containing proteins and the mechanisms by which the apo-protein structure controls chemical reactivity, presents a major experimental and theoretical challenge. These issues are discussed in the general context of peroxidase and cytochrome P450 chemistry, and specific issues relating to the catalytic chemistry of ascorbate peroxidase are highlighted.

摘要

理解血红素酶的催化多样性,尤其是不同种类含血红素蛋白质之间存在的关系以及脱辅基蛋白结构控制化学反应性的机制,是一项重大的实验和理论挑战。本文将在过氧化物酶和细胞色素P450化学的总体背景下讨论这些问题,并着重强调与抗坏血酸过氧化物酶催化化学相关的具体问题。

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