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.

引用

页码：421 / 431

页数：11

共 18 条

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