Fluctuating enzymes: Lessons from single-molecule studies

被引：316

作者：

Min, W

English, BP

Luo, GB

Cherayil, BJ

Kou, SC

Xie, XS ^{[1
]}

机构：

[1] Harvard Univ, Dept Chem & Chem Biol, Cambridge, MA 02138 USA

[2] Harvard Univ, Dept Stat, Cambridge, MA 02138 USA

来源：

ACCOUNTS OF CHEMICAL RESEARCH | 2005年 / 38卷 / 12期

关键词：

D O I：

10.1021/ar040133f

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Recent single-molecule enzymology measurements with improved statistics have demonstrated that a single enzyme molecule exhibits large temporal fluctuations of the turnover rate constant at a broad range of time scales (from 1 ms to 100 s). The rate constant fluctuations, termed as dynamic disorder, are associated with fluctuations of the protein conformations observed on the same time scales. We discuss the unique information extractable from these experiments and the reconciliation of these observations with ensemble-averaged Michaelis-Menten equation. A theoretical model based on the generalized Langevin equation (GLE) treatment of Kramers' barrier crossing problem for chemical reactions accounts naturally for the observation of dynamic disorder and highly dispersed kinetics.

引用

页码：923 / 931

页数：9

共 59 条

[1] Kinesin moves by an asymmetric hand-over-hand mechanism [J].