THE REDOX MIDPOINT POTENTIAL OF HEME-A IN CYTOCHROME-C OXIDASE IS SENSITIVE TO EXTRAMITOCHONDRIAL PH

被引：4

作者：

MITCHELL, JR ^{[1
]}

MITCHELL, P ^{[1
]}

机构：

[1] GLYNN RES INST,CORNWALL PL30 4AU,ENGLAND

来源：

BIOCHEMICAL SOCIETY TRANSACTIONS | 1989年 / 17卷 / 05期

关键词：

D O I：

10.1042/bst0170892

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：

引用

页码：892 / 893

页数：2

共 7 条

[1]

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MOODY, AJ ;

MITCHELL, R ;

RICH, PR .

BIOCHEMICAL SOCIETY TRANSACTIONS, 1989, 17 (05) :895-896

[3] REDOX TITRATION OF HEME-A IN CYANIDE-LIGANDED CYTOCHROME-C OXIDASE - SIMULATION STUDIES ON INTERACTING, PH-DEPENDENT, REDOX CENTERS [J].

MOODY, AJ ;

RICH, PR .

BIOCHEMICAL SOCIETY TRANSACTIONS, 1989, 17 (05) :896-897

[4] EFFECT OF MEMBRANE-POTENTIAL AND PH GRADIENT ON ELECTRON-TRANSFER IN CYTOCHROME-OXIDASE [J].

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[5] PROTON-PUMPING CYTOCHROME-C OXIDASE [J].

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KRAB, K .

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[6]

Wikstrom M, 1985, ENZYMES BIOL MEMBR, V4, P111

[7] ACTIVATION BY REDUCTION OF THE RESTING FORM OF CYTOCHROME-C OXIDASE - TESTS OF DIFFERENT MODELS AND EVIDENCE FOR THE INVOLVEMENT OF CUB [J].

WRIGGLESWORTH, JM ;

ELSDEN, J ;

CHAPMAN, A ;

VANDERWATER, N ;

GRAHN, MF .

BIOCHIMICA ET BIOPHYSICA ACTA, 1988, 936 (03) :452-464

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