High-accuracy computation of reaction barriers in enzymes

被引：217

作者：

Claeyssens, Frederik

Harvey, Jeremy N.

Manby, Frederick R.

Mata, Ricardo A.

Mulholland, Adrian J.

Ranaghan, Kara E.

Schuetz, Martin

Thiel, Stephan

Thiel, Walter

Werner, Hans-Joachim

机构：

[1] Univ Bristol, Sch Chem, Bristol BS8 1TS, Avon, England

[2] Max Planck Inst Kohlenforsch, D-45470 Mulheim, Germany

[3] Univ Stuttgart, Inst Theoret Chem, D-70569 Stuttgart, Germany

[4] Univ Regensburg, Inst Phys & Theoret Chem, D-93040 Regensburg, Germany

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2006年 / 45卷 / 41期

基金：

英国工程与自然科学研究理事会;

关键词：

ab initio calculations; enzyme catalysis; QM/MM calculations; reaction mechanisms; transition-state theory;

D O I：

10.1002/anie.200602711

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Modeling enzyme catalysis: High-level ab initio QM/MM calculations yield activation enthalpies and free energies for chorismate mutase and pora-hydroxybenzoate hydroxylase that are in excellent agreement with experimental results. Enzyme reactivity is described quantitatively by transition-state theory. (Figure Presented) © 2006 Wiley-VCH Verlag GmbH & Co. KGaA.

引用

页码：6856 / 6859

页数：4

共 29 条

[1] DENSITY-FUNCTIONAL THERMOCHEMISTRY .3. THE ROLE OF EXACT EXCHANGE [J].