Literature summary for 7.1.1.9 extracted from

Mason, M.G.; Nicholls, P.; Wilson, M.T.; Cooper, C.E.
Nitric oxide inhibition of respiration involves both competitive (heme) and noncompetitive (copper) binding to cytochrome c oxidase (2006), Proc. Natl. Acad. Sci. USA, 103, 708-713.

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Inhibitors

Inhibitors	Comment	Organism	Structure
nitric oxide	steady-state and kinetic modeling of inhibition. NO interacts with either ferrous heme iron or oxidized copper, but not both simultaneously. The affinity of NO for the oxygen-binding ferrous heme site is 0.2 nM	Bos taurus

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Cu2+	interaction of inhibitor nitric oxide is either with ferrous heme iron or oxidized copper, but not both simultaneously. The noncompetitive interaction with oxidized copper results in oxidation of NO to nitrite and behaves kinetically as if it has an apparent affinity of 28 nM	Bos taurus
Fe2+	interaction of inhibitor nitric oxide is either with ferrous heme iron or oxidized copper, but not both simultaneously. The affinity of NO for the oxygen-binding ferrous heme site is 0.2 nM	Bos taurus

Organism

Organism	UniProt	Comment	Textmining
Bos taurus	-	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
heart	-	Bos taurus	-

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Release 2023.1 (January 2023)