The inhibitory binding site(s) of Zn2+ in cytochrome c oxidase

EXAFS identifies 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 redu...

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Veröffentlicht in:	FEBS letters 2007-02, Vol.581 (4), p.611-616
Hauptverfasser:	Francia, Francesco, Giachini, Lisa, Boscherini, Federico, Venturoli, Giovanni, Capitanio, Giuseppe, Martino, Pietro Luca, Papa, Sergio
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Binding Sites - drug effects carbonyl cyanide m-chlorophenylhydrazone Cattle CCCP Cell Membrane - drug effects Cell Membrane - enzymology Cytochrome c oxidase Electron Transport - drug effects Electron Transport Complex IV - antagonists & inhibitors Electron Transport Complex IV - chemistry Electron Transport Complex IV - metabolism Horses Liposomes Models, Molecular Protein Subunits - chemistry Protein Subunits - metabolism Protein Zn binding Proton pumping Proton Pumps - drug effects Protons Zinc - metabolism Zinc - pharmacology
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Zusammenfassung:	EXAFS identifies 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.
ISSN:	0014-5793 1873-3468
DOI:	10.1016/j.febslet.2007.01.017