Site-specific conversion of cysteine thiols into thiocyanate creates an IR probe for electric fields in proteins

被引：186

作者：

Fafarman, Aaron T. ^{[1
]}

Webb, Lauren J. ^{[1
]}

Chuang, Jessica I. ^{[1
]}

Boxer, Steven G. ^{[1
]}

机构：

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

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2006年 / 128卷 / 41期

关键词：

D O I：

10.1021/ja0650403

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

The nitrile stretching mode of the thiocyanate moiety is a nearly ideal probe for measuring the local electric field arising from the organized environment of the interior of a protein. Nitriles were introduced into three proteins: ribonuclease S (RNase S), human aldose reductase (hALR2), and the reaction center (RC) of Rhodobacter capsulatus, through a facile synthetic scheme for the transformation of cysteine residues into thiocyanatoalanine. Vibrational Stark effect spectroscopy and Fourier transform infrared spectroscopy on the modified proteins demonstrated that thiocyanate residues are a highly general tool for probing electrostatic fields in proteins. Copyright © 2006 American Chemical Society.

引用

页码：13356 / 13357

页数：2

共 23 条

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