Multiple-steering QM-MM calculation of the free energy profile in chorismate mutase

被引：100

作者：

Crespo, A

Martí, MA

Estrin, DA ^{[1
]}

Roitberg, AE

机构：

[1] Univ Florida, Quantum Theory Project, Gainesville, FL 32611 USA

[2] Univ Florida, Dept Chem, Gainesville, FL 32611 USA

[3] Univ Buenos Aires, Fac Ciencias Exactas & Nat, Dept Quim Inorgan Analit & Quim Fis, RA-1428 Buenos Aires, DF, Argentina

[4] Univ Buenos Aires, Fac Ciencias Exactas & Nat, CONICET, INQUIMAE, RA-1428 Buenos Aires, DF, Argentina

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2005年 / 127卷 / 19期

关键词：

D O I：

10.1021/ja0452830

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

A novel technique for computing free energy profiles in enzymatic reactions using the multiple steering molecular dynamics approach in the context of an efficient QM-MM density functional scheme is presented. The conversion reaction of chorismate to prephenate catalyzed by the Bacillus subtilis enzyme chorismate mutase has been chosen as an illustrative example. Copyright © 2005 American Chemical Society.

引用

页码：6940 / 6941

页数：2

共 12 条

[11] Accelerating rare reactive events by means of a finite electronic temperature [J].