Examining the case for the effect of barrier compression on tunneling, vibrationally enhanced catalysis, catalytic entropy and related issues

被引：70

作者：

Kamerlin, Shina Caroline Lynn ^{[1
]}

Mavri, Janez ^{[2
]}

Warshel, A. ^{[1
]}

机构：

[1] Univ So Calif, Dept Chem SGM418, Los Angeles, CA 90089 USA

[2] Natl Inst Chem, SI-1001 Ljubljana, Slovenia

来源：

FEBS LETTERS | 2010年 / 584卷 / 13期

基金：

美国国家卫生研究院;

关键词：

Enzyme catalysis; Tunneling; Barrier compression; Promoting mode; Kinetic isotope effect; Catalytic entropy; TRANSITION-STATE STABILIZATION; PROTEIN PROMOTING VIBRATION; ENZYME CATALYSIS; CHORISMATE MUTASE; ALCOHOL-DEHYDROGENASE; DIHYDROFOLATE-REDUCTASE; MOLECULAR-DYNAMICS; HYDRIDE TRANSFER; O-H; PRESSURE;

D O I：

10.1016/j.febslet.2010.04.062

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The idea that tunneling is enhanced by the compression of the donor-acceptor distance has attracted significant interest. In particular, recent studies argued that this proposal is consistent with pressure effects on enzymatic reactions, and that the observed pressure effects support the idea of vibrationally enhanced catalysis. However, a careful analysis of the current works reveals serious inconsistencies in the evidence presented to support these hypotheses. Apparently, tunneling decreases upon compression, and external pressure does not lead to the applicable compression of the free energy surface. Additionally, pressure experiments do not provide actual evidence for vibrationally enhanced catalysis. Finally, the temperature dependence of the entropy change in hydride transfer reactions is shown to reflect simple electrostatic effects. (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.

引用

页码：2759 / 2766

页数：8