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Literature summary for 7.1.1.9 extracted from

  • Cooper, C.E.; Davies, N.A.; Psychoulis, M.; Canevari, L.; Bates, T.E.; Dobbie, M.S.; Casley, C.S.; Sharpe, M.A.
    Nitric oxide and peroxynitrite cause irreversible increases in the K(m) for oxygen of mitochondrial cytochrome oxidase: in vitro and in vivo studies (2003), Biochim. Biophys. Acta, 1607, 27-34.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
CO competitive and reversible Bos taurus
nitric oxide competitive and reversible. Nanomolar levels inhibit the enzyme by competing with oxygen at the enzyme‘s heme-copper active site. This raises the Km for cellular respiration into the physiological range Bos taurus

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
Bos taurus 5739
-

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
heart
-
Bos taurus
-