Literature summary for 7.1.1.9 extracted from

Parihar, A.; Vaccaro, P.; Ghafourifar, P.
Nitric oxide irreversibly inhibits cytochrome oxidase at low oxygen concentrations: evidence for inverse oxygen concentration-dependent peroxynitrite formation (2008), IUBMB Life, 60, 64-67.

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Inhibitors

Inhibitors	Comment	Organism	Structure
NO	irreversibly inhibits in a reverse oxygen concentration-dependent manner. COX activity is decreased from 51.3% at 0.2 mM and to 3.8% at 0.025 mM. Inhibition is dramatically protected by a peroxynitrite scavenger, which is formed from the reaction of NO with cytochrome oxidase at low oxygen concentration, and that is involved in irreversible cytochrome oxidase inactivation. Nitroxyl anion scavenger potently protects the irreversible inhibition, whereas a superoxide dismutase does not provide protective effect, suggesting that the peroxynitrite is formed from nitroxyl anion rather than the reaction of NO with superoxide	Rattus norvegicus

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
mitochondrial inner membrane	-	Rattus norvegicus	5743	-

Organism

Organism	UniProt	Comment	Textmining
Rattus norvegicus	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
by differential solubilization	Rattus norvegicus

Source Tissue

Source Tissue	Comment	Organism	Textmining
liver	-	Rattus norvegicus	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
reduced cytochrome c + O2 + H+	-	Rattus norvegicus	oxidized cytochrome c + H2O	-	?

Synonyms

Synonyms	Comment	Organism
COX	-	Rattus norvegicus
cytochrome c oxidase	-	Rattus norvegicus
cytochrome oxidase	-	Rattus norvegicus

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Release 2023.1 (January 2023)