Conformational cycle of a single working enzyme

被引：75

作者：

Agmon, N ^{[1
]}

机构：

[1] Hebrew Univ Jerusalem, Fritz Haber Res Ctr, Dept Chem Phys, IL-91904 Jerusalem, Israel

来源：

JOURNAL OF PHYSICAL CHEMISTRY B | 2000年 / 104卷 / 32期

关键词：

D O I：

10.1021/jp0012911

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

By simultaneous analysis of the on-time distribution and autocorrelation function of a single working cholesterol oxidase enzyme, a diffusional model reveals the coupling of conformation change with enzyme action. Active-site oxidation induces a conformational change that opens the path for substrate entry. Its binding, in turn, induces the reverse protein relaxation process, which tightens the active site, thereby reducing the rate of product release.

引用

页码：7830 / 7834

页数：5

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