Hydrogen tunneling in peptidylglycine α-hydroxylating monooxygenase

被引：108

作者：

Francisco, WA

Knapp, MJ

Blackburn, NJ

Klinman, JP ^{[1
]}

机构：

[1] Univ Calif Berkeley, Dept Chem, Berkeley, CA 94720 USA

[2] Univ Calif Berkeley, Dept Mol & Cell Biol, Berkeley, CA 94720 USA

[3] Oregon Grad Inst Sci & Technol, Dept Biochem & Mol Biol, Beaverton, OR 97006 USA

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2002年 / 124卷 / 28期

关键词：

D O I：

10.1021/ja025758s

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

The temperature dependence of the primary and secondary intrinsic isotope effects for the C-H bond cleavage catalyzed by peptidylglycine α-hydroxylating monooxygenase has been determined. Analysis of the magnitude and Arrhenius behavior of the intrinsic isotope effects provides strong evidence for the use of tunneling as a primary catalytic strategy for this enzyme. Modeling of the isotope effect data allows for a comparison to the hydrogen transfer catalyzed by soybean lipoxygenase in terms of environmental reorganization energy and frequency of the protein vibration that controls the hydrogen transfer. Copyright © 2002 American Chemical Society.

引用

页码：8194 / 8195

页数：2

共 28 条

[11] EVIDENCE THAT BOTH PROTIUM AND DEUTERIUM UNDERGO SIGNIFICANT TUNNELING IN THE REACTION CATALYZED BY BOVINE SERUM AMINE OXIDASE [J].