Molecular dynamics of an enzyme reaction: Proton transfer in TIM

被引：90
作者：
Neria, E [1 ]
Karplus, M [1 ]
机构：
[1] UNIV STRASBOURG 1,INST LE BEL,LAB CHIM BIOPHYS,F-67000 STRASBOURG,FRANCE
来源：
CHEMICAL PHYSICS LETTERS | 1997年 / 267卷 / 1-2期
基金：
美国国家科学基金会;
关键词：
D O I：
10.1016/S0009-2614(97)00068-7
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：
The initial proton transfer step in the reaction catalyzed by the enzyme triosephosphate isomerase is examined by activated dynamics simulations. The transmission coefficient, kappa, which corrects the transition-state theory (TST) rate constant for recrossings of the activation barrier, is calculated to be 0.4, relative to the TST value of unity. Medium effects on the dynamics in the enzyme an compared with those on charge transfer reactions in solution.
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页码：23 / 30
页数：8
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