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Titolo:
CELL RESPIRATION IS CONTROLLED BY ATP, AN ALLOSTERIC INHIBITOR OF CYTOCHROME-C-OXIDASE
Autore:
ARNOLD S; KADENBACH B;
Indirizzi:
UNIV MARBURG,FACHBEREICH CHEM,HANS MEERWEIN STR D-35032 MARBURG GERMANY UNIV MARBURG,FACHBEREICH CHEM D-35032 MARBURG GERMANY
Titolo Testata:
European journal of biochemistry
fascicolo: 1, volume: 249, anno: 1997,
pagine: 350 - 354
SICI:
0014-2956(1997)249:1<350:CRICBA>2.0.ZU;2-S
Fonte:
ISI
Lingua:
ENG
Soggetto:
BOVINE HEART; OXIDATIVE-PHOSPHORYLATION; MITOCHONDRIAL-MEMBRANE; PHOSPHATE METABOLITES; ELECTRON-TRANSFER; 2.8 ANGSTROM; BINDING; KINETICS; 8-AZIDO-ATP; CARDIOLIPIN;
Keywords:
CYTOCHROME-C OXIDASE; ALLOSTERIC ENZYME; ATP/ADP RATIO; HILL COEFFICIENT; CARDIOLIPIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
39
Recensione:
Indirizzi per estratti:
Citazione:
S. Arnold e B. Kadenbach, "CELL RESPIRATION IS CONTROLLED BY ATP, AN ALLOSTERIC INHIBITOR OF CYTOCHROME-C-OXIDASE", European journal of biochemistry, 249(1), 1997, pp. 350-354

Abstract

The activity of cytochrome-c oxidase, the terminal enzyme of the mitochondrial respiratory chain, is known to be regulated by the substratepressure, i.e. the ferro-/ferricytochrome c ratio, by the oxygen concentration, and by the electrochemical proton gradient Delta mu(H+) across the inner mitochondrial membrane. Here we describe a further mechanism of 'respiratory control' via allosteric inhibition of cytochrome-c oxidase by ATP, which binds to the matrix domain, of subunit IV. Thecooperativity between cytochrome-c-binding sites in the dimeric enzyme complex is mediated by cardiolipin, which is essential for cooperativity of the enzyme within the lipid membrane.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 19/09/20 alle ore 12:50:50