RESONANCE RAMAN-SPECTROSCOPIC STUDIES OF ENZYME-SUBSTRATE INTERMEDIATES AT 5-K

被引：9
|
作者：
KIM, MS [1 ]
CAREY, PR [1 ]
机构：
[1] NATL RES COUNCIL CANADA,INST BIOL SCI,OTTAWA K1A 0R6,ONTARIO,CANADA
来源：
JOURNAL OF MOLECULAR STRUCTURE | 1991年 / 242卷
关键词：
D O I：
10.1016/0022-2860(91)87152-8
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：
A simple and versatile system for resonance Raman (RR) spectroscopic analysis of enzyme-substrate complexes at liquid helium temperatures is described. The system allows us to record high-quality RR spectra for dithioacyl papain intermediates (MeO-Phe-Gly- and MeO-Gly-Gly-Phe-Gly-C(= S)S-papain) in ice matrices at 5 K. Based on established structure-spectra correlations, it is concluded that the active-site conformation of the intermediates about the phi', psi' glycinic linkages and cysteine-25 side chain is B-G+-P(H) both in ice matrices at 5 K and in solution at room temperature.
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页码：421 / 431
页数：11
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