RESONANCE RAMAN-SPECTROSCOPY REVEALS NOVEL LIGATION PROPERTIES OF THE PORCINE MYOGLOBIN DOUBLE MUTANT H64V/V68H

被引：6

作者：

ANDERTON, CL ^{[1
]}

HESTER, RE ^{[1
]}

MOORE, JN ^{[1
]}

机构：

[1] UNIV YORK,DEPT CHEM,YORK YO1 5DD,N YORKSHIRE,ENGLAND

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY | 1995年 / 1253卷 / 01期

基金：

英国工程与自然科学研究理事会;

关键词：

RESONANCE RAMAN SPECTROSCOPY; LIGATION; DOUBLE MUTANT; MYOGLOBIN (PORCINE);

D O I：

10.1016/0167-4838(95)00177-V

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A resonance Raman spectroscopic study of the porcine myoglobin double mutant H64V/V68H has confirmed that the ferric form is bis-histidine ligated, has revealed that the bis-histidine ligation is retained on reduction to the ferrous form, and has demonstrated that CO can displace the ligated distal histidine to produce a ferrous CO form which has a low steady-state photolability, indicating that the replacement histidine blocks the CO escape route from the binding site.

引用

页码：1 / 4

页数：4

共 26 条

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