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Titolo:
Kinetic mechanism of ATP synthesis catalyzed by mitochondrial F-0 center dot F-1-ATPase
Autore:
Galkin, MA; Syroeshkin, AV;
Indirizzi:
Moscow MV Lomonosov State Univ, Sch Biol, Dept Biochem, Moscow 119899, Russia Moscow MV Lomonosov State Univ Moscow Russia 119899 oscow 119899, Russia
Titolo Testata:
BIOCHEMISTRY-MOSCOW
fascicolo: 10, volume: 64, anno: 1999,
pagine: 1176 - 1185
SICI:
0006-2979(199910)64:10<1176:KMOASC>2.0.ZU;2-A
Fonte:
ISI
Lingua:
ENG
Soggetto:
STEADY-STATE KINETICS; CHLOROPLAST COUPLING FACTOR; BOVINE HEART-MITOCHONDRIA; ENZYME-BOUND ATP; OXIDATIVE-PHOSPHORYLATION; ADENOSINE-TRIPHOSPHATASE; STRUCTURAL ASYMMETRY; F1-ATPASE; SYNTHASE; ADP;
Keywords:
F-0 center dot F-1-ATPase; mitochondrion; Delta(mu)over-bar(H)+-dependent ATP synthesis;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
54
Recensione:
Indirizzi per estratti:
Indirizzo: Galkin, MA Moscow MV Lomonosov State Univ, Sch Biol, Dept Biochem, Moscow 119899, Russia Moscow MV Lomonosov State Univ Moscow Russia 119899 9, Russia
Citazione:
M.A. Galkin e A.V. Syroeshkin, "Kinetic mechanism of ATP synthesis catalyzed by mitochondrial F-0 center dot F-1-ATPase", BIOCHEM-MOS, 64(10), 1999, pp. 1176-1185

Abstract

Initial rates of succinate-dependent ATP synthesis catalyzed by submitochondrial particles from bovine heart substoichiometrically coupled with oligomycin were found to have hyperbolic dependencies on contents of Mg ADP, free Mg2+, and phosphate. The results suggest that Mg.ADP complex and free phosphate are true substrates of the enzyme; and an unordered tertiary complexof F-0.F-1-ATPase, Mg.ADP, and phosphate is generated during the catalysis. The presence of free Mg2+ is required for the reaction. Mg2+ was a noncompetitive activator of ATP synthesis relative to Mg.ADP and a competitive activator relative to phosphate. The decrease in steady-state values of Deltamu(H+) (by the inhibition of succinate oxidase with malonate) results in the decreased value of V-max and in a slight decrease in K-m for the substrates and Mg2+ without changes in affinity for the substrates. Based on theseresults, a kinetic scheme of ATP synthesis is proposed.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/11/20 alle ore 05:00:17