STRUCTURAL AND ENZYMOLOGICAL ANALYSIS OF THE INTERACTION OF ISOLATED DOMAINS OF CYTOCHROME-P-450 BM3

被引：49

作者：

MUNRO, AW ^{[1
]}

LINDSAY, JG ^{[1
]}

COGGINS, JR ^{[1
]}

KELLY, SM ^{[1
]}

PRICE, NC ^{[1
]}

机构：

[1] UNIV STIRLING,DEPT BIOL & MOLEC SCI,STIRLING FK9 4LA,SCOTLAND

来源：

FEBS LETTERS | 1994年 / 343卷 / 01期

关键词：

CYTOCHROME-P-450-BM3; DOMAIN INTERACTION; CIRCULAR DICHROISM; ELECTRON TRANSFER; HEME ENVIRONMENT;

D O I：

10.1016/0014-5793(94)80609-8

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：

The interactions of the individually expressed haem- and flavin-containing domains of cytochrome P-450 BM3 have been analysed by enzymological and spectroscopic techniques. Electron transfer between the isolated domains occurs at a much lower rate than that occurring in the intact flavocytochrome. CD spectroscopic studies indicate that the linkage of the domains in intact P-450 BM3 creates haem and amino acid environments suitable for efficient electron transfer from its flavin domain.

引用

页码：70 / 74

页数：5