Inhibition of plant and animal cytochrome oxidases by nitrous oxide as a function of cytochrome c concentration

Cytochrome oxidase from both pea leaves and bovine heart shows lower activity under a mixture of 79% N 2O/21% O 2 than under ambient air. This inhibition is not detectable below 5 μM cytochrome c but appears with increasing concentrations of cytochrome c. This seems to concern only the lowest site o...

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Veröffentlicht in:	Biochimie 1992-12, Vol.74 (12), p.1125-1127
Hauptverfasser:	Chervin, C., Thibaud, M.C.
Format:	Artikel
Sprache:	eng
Schlagworte:	anaesthetic Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Cattle Cytochrome c Group - metabolism cytochrome c oxidase Electron Transport Complex IV - antagonists & inhibitors Electron Transport Complex IV - metabolism Enzymes and enzyme inhibitors Fabaceae Fundamental and applied biological sciences. Psychology Life Sciences mitochondria Myocardium - enzymology nitrous oxide Nitrous Oxide - pharmacology Octoxynol Oxidoreductases Plants - enzymology Plants, Medicinal Polyethylene Glycols
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Zusammenfassung:	Cytochrome oxidase from both pea leaves and bovine heart shows lower activity under a mixture of 79% N 2O/21% O 2 than under ambient air. This inhibition is not detectable below 5 μM cytochrome c but appears with increasing concentrations of cytochrome c. This seems to concern only the lowest site of the oxidase. Apparently, N 2O and cytochrome c do not share the concentration. This seems to concern only the lowest affinity site of the oxidase. Apparently, N 2O and cytochrome c do not share the same site of fixation on the oxidase.
ISSN:	0300-9084 1638-6183
DOI:	10.1016/0300-9084(92)90012-4