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Titolo:
REGULATION OF ENERGY TRANSDUCTION AND ELECTRON-TRANSFER IN CYTOCHROME-C-OXIDASE BY ADENINE-NUCLEOTIDES
Autore:
KADENBACH B; NAPIWOTZKI J; FRANK V; ARNOLD S; EXNER S; HUTTEMANN M;
Indirizzi:
UNIV MARBURG,FACHBEREICH CHEM D-35032 MARBURG GERMANY
Titolo Testata:
Journal of bioenergetics and biomembranes
fascicolo: 1, volume: 30, anno: 1998,
pagine: 25 - 33
SICI:
0145-479X(1998)30:1<25:ROETAE>2.0.ZU;2-3
Fonte:
ISI
Lingua:
ENG
Soggetto:
SPECIES-SPECIFIC EXPRESSION; TISSUE-SPECIFIC REGULATION; BOVINE HEART; SUBUNIT-V; CONFORMATIONAL-CHANGES; BINDING-SITES; 2.8 ANGSTROM; MITOCHONDRIAL; KINETICS; ISOZYMES;
Keywords:
CYTOCHROME C OXIDASE; H+/E(-) STOICHIOMETRY; THERMOGENESIS; ADENINE NUCLEOTIDES; REGULATION OF ACTIVITY; ECTOTHERM ANIMALS; ATP/ADP RATIOS; ALLOSTERIC ENZYME; MONOCLONAL ANTIBODIES; RATE OF RESPIRATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
57
Recensione:
Indirizzi per estratti:
Citazione:
B. Kadenbach et al., "REGULATION OF ENERGY TRANSDUCTION AND ELECTRON-TRANSFER IN CYTOCHROME-C-OXIDASE BY ADENINE-NUCLEOTIDES", Journal of bioenergetics and biomembranes, 30(1), 1998, pp. 25-33

Abstract

Cytochrome c oxidase from bovine heart contains seven high-affinity binding sites for ATP or ADP and three additional only for ADP. One binding site for ATP or ADP, located at the matrix-oriented domain of theheart-type subunit VIaH, increases the H+/e(-) stoichiometry of the enzyme from heart or skeletal muscle from 0.5 to 1.0 when bound ATP is exchanged by ADP. Two further binding sites for ATP or ADP, located atthe cytosolic and the matrix domain of subunit IV, increases the KM for cytochrome c and inhibit the respiratory activity at high ATP/ADP ratios, respectively. We propose that thermogenesis in mammals is related to subunit VIaL of cytochrome c oxidase with a H+/e(-) stoichiometry of 0.5 compared to 1.0 in the enzyme from bacteria or ectotherm animals. This hypothesis is supported by the lack of subunit VIa isoforms in cytochrome c oxidase from fish.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 19/09/20 alle ore 12:39:43