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.

Cytochrome c oxidase does not catalyze the anaerobic reduction of NO

Giuffrè A;
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.
1998
Istituto di Biologia e Patologia Molecolari - IBPM
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
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/20.500.14243/241577
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