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The inhibitory binding site(s) of Zn 2+ in cytochrome c oxidase
Author(s) -
Francia Francesco,
Giachini Lisa,
Boscherini Federico,
Venturoli Giovanni,
Capitanio Giuseppe,
Martino Pietro Luca,
Papa Sergio
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.01.017
Subject(s) - chemistry , cytochrome c oxidase , histidine , zinc , oxidase test , extended x ray absorption fine structure , binding site , active site , catalysis , stereochemistry , inorganic chemistry , enzyme , biochemistry , absorption spectroscopy , organic chemistry , quantum mechanics , physics
EXAFS identifies tetrahedral coordination site(s) for Zn 2+ 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.