Data di Pubblicazione:
1998
Abstract:
A possible role of reduced cytochrome c oxidase in the metabolism of nitric oxide (NO) has been examined with amperometric and stopped-flow photometric techniques. Reduced purified cytochrome c oxidase and mitochondria showed no catalytic reaction with NO under anaerobic conditions within more than 30 minutes. Only fast binding of NO to the reduced enzyme in a 1:1 stoichiometric ratio was observed. The NO binding rate was strongly decreased in the presence of 1 mM cyanide. These data indicate that, contrary to previous proposals, cytochrome c oxidase in the absence of oxygen does not contribute to physiological NO metabolism.
Tipologia CRIS:
01.01 Articolo in rivista
Keywords:
cyanide; cytochrome c oxidase; nitric oxide; amperometry; anaerobic metabolism; animal tissue; article; controlled study; enzyme binding; nonhuman; photometry; priority journal; reduction; stoichiometry; Anaerobiosis; Animals; Ascorbic Acid; Cattle; Electrochemistry; Electron Transport Complex IV; Kinetics; Mitochondria; Heart; Nitric Oxide; Oxidation-Reduction; Protein Binding; Regression Analysis; Ruthenium Compounds; Sodium Cyanide; Spectrophotometry
Elenco autori:
Brunori, Maurizio; Giuffre', Alessandro
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