Literature summary for 7.1.1.9 extracted from

Francia, F.; Giachini, L.; Boscherini, F.; Venturoli, G.; Capitanio, G.; Martino, P.L.; Papa, S.
The inhibitory binding site(s) of Zn2+ in cytochrome c oxidase (2007), FEBS Lett., 581, 611-616.

Search for more literature for 7.1.1.9

Inhibitors

Inhibitors	Comment	Organism	Structure
Zn2+	tetrahedral coordination of Zn2+ with two N-histidine imidazoles, one N-histidine imidazol or N-lysine and one O-COOH, possibly located at the entry site ogf the proton conducting D pathway; tetrahedral coordination site(s) for Zn2+ with two N-histidine imidazoles, one N-histidine imidazol or N-lysine and one O-COOH (glutamate or aspartate), possibly located at the entry site of the proton conducting D pathway in the oxidase and involved in inhibition of the oxygen reduction catalysis and proton pumping by internally trapped zinc. Presence of ZnCl2 during liposome reconstitution of cytochrome c oxidase has no effect on the sidedness of the incorporated COX, neither increases the residual amount of soluble COX	Bos taurus

Organism

Organism	UniProt	Comment	Textmining
Bos taurus	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Bos taurus

Source Tissue

Source Tissue	Comment	Organism	Textmining
heart	-	Bos taurus	-

Synonyms

Synonyms	Comment	Organism
COX	-	Bos taurus
cytochrome c oxidase	-	Bos taurus

Cofactor

Cofactor	Comment	Organism	Structure
heme	-	Bos taurus

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)