Site-specific conversion of cysteine thiols into thiocyanate creates an IR probe for electric fields in proteins
Site-specific conversion of cysteine thiols into thiocyanate creates an IR probe for electric fields in proteins
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DOI：
10.1021/ja0650403
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发表时间：
2006-10-18
影响因子：
15
通讯作者：
Boxer, Steven G.
中科院分区：
文献类型：
--
作者：
Fafarman, Aaron T.;Webb, Lauren J.;Boxer, Steven G.
硫氰酸盐部分的氰基伸缩模式是测量蛋白质内部有组织环境产生的局部电场的近乎理想的探头。通过一种简便的将半胱氨酸残基转化为硫氰酸丙氨酸的合成方案，将腈引入三种蛋白质： 核糖核酸酶S(核糖核酸酶S)、人醛糖还原酶(HALR2)和胶囊红杆菌的反应中心(RC)。对修饰蛋白质的振动斯塔克效应光谱和傅里叶变换红外光谱表明，硫氰酸盐残基是探测蛋白质中静电场的一种非常通用的工具。
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) ofRhodobacter 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.