Electric fields at the active site of an enzyme: Direct comparison of experiment with theory

被引：292

作者：

Suydam, Ian T. ^{[1
]}

Snow, Christopher D. ^{[1
]}

Pande, Vijay S. ^{[1
]}

Boxer, Steven G. ^{[1
]}

机构：

[1] Stanford Univ, Dept Chem, Stanford, CA 94305 USA

来源：

SCIENCE | 2006年 / 313卷 / 5784期

关键词：

D O I：

10.1126/science.1127159

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The electric fields produced in folded proteins influence nearly every aspect of protein function. We present a vibrational spectroscopy technique that measures changes in electric field at a specific site of a protein as shifts in frequency ( Stark shifts) of a calibrated nitrile vibration. A nitrile-containing inhibitor is used to deliver a unique probe vibration to the active site of human aldose reductase, and the response of the nitrile stretch frequency is measured for a series of mutations in the enzyme active site. These shifts yield quantitative information on electric fields that can be directly compared with electrostatics calculations. We show that extensive molecular dynamics simulations and ensemble averaging are required to reproduce the observed changes in field.

引用

页码：200 / 204

页数：5

共 27 条

[1] Vibrational Stark effects of nitriles II. Physical origins of stark effects from experiment and perturbation models [J].