Proton dynamics in an enzyme model substrate: an ab initio molecular dynamics study

被引：14

作者：

Pantano, S

Alber, F

Carloni, P

机构：

[1] Int Ctr Genet Engn & Biotechnol, I-34012 Trieste, Italy

[2] Scuola Int Super Studi Avanzati, SISSA, I-34014 Trieste, Italy

[3] Ist Nazl Fis Mat, I-34014 Trieste, Italy

来源：

JOURNAL OF MOLECULAR STRUCTURE-THEOCHEM | 2000年 / 530卷 / 1-2期

关键词：

ab initio molecular dynamics; low-barrier-hydrogen-bond; proton transfer; finite temperature effects; enolic intermediate;

D O I：

10.1016/S0166-1280(00)00331-6

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：

We have investigated theoretically the influence of thermal fluctuations on the proton hopping properties of a model substrate for enzymatic reactions, benzoylacetone. Our calculations, based on the Car-Parrinello molecular dynamics approach, indicate that proton transfer events occur on a very short time scale and they are accompanied by a concerted motion of the H-bond donors towards the hydrogen. Possible implications of the latter finding for enzyme mechanism of action are discussed. (C) 2000 Elsevier Science B.V. All rights reserved.

引用

页码：177 / 181

页数：5

共 35 条

[1]

AHS EL, 1997, SCIENCE, V278, P1128

[2] Conformational analysis of dimethyl phosphate in aqueous solution: a density functional theory-based molecular dynamics study [J].