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一个用于酶催化的综合模型源自对氢隧穿的研究。

An integrated model for enzyme catalysis emerges from studies of hydrogen tunneling.

作者信息

Klinman Judith P

机构信息

Departments of Chemistry and Molecular and Cell Biology, University of California, Berkeley, CA 94720-1460, USA.

出版信息

Chem Phys Lett. 2009 Mar 26;471(4-6):179-193. doi: 10.1016/j.cplett.2009.01.038.

Abstract

The origins of the enormous rate accelerations brought about by enzymes are discussed. The focus is on enzymatic C-H activation, which has been shown to take place via tunneling. Four enzyme systems illustrate the impact of site-specific mutagenesis, changes in temperature or changes in protein solvation on the tunneling properties. A model emerges in which conformational sampling is required to access a subset of protein conformers where the H-donor and acceptor undergo a close approach. The evidence for an inverse relationship between protein flexibility and active site compression is likely to extend to all classes of enzyme catalysts.

摘要

本文讨论了酶所带来的巨大速率加速的起源。重点是酶促C-H活化,已证明其通过隧穿发生。四个酶系统说明了位点特异性诱变、温度变化或蛋白质溶剂化变化对隧穿性质的影响。由此出现了一个模型,其中需要进行构象采样以获取蛋白质构象体的一个子集,在该子集中氢供体和受体紧密靠近。蛋白质柔韧性与活性位点压缩之间呈反比关系的证据可能适用于所有类型的酶催化剂。

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