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A Functional Model of Cytochrome c Oxidase: Thermodynamic Implications
Author(s) -
Collman James P.,
Fu Lei,
Herrmann Paul C.,
Wang Zhong,
Rapta Miroslav,
Bröring Martin,
Schwenninger Reinhold,
Boitrel Bernard
Publication year - 1998
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/(sici)1521-3773(19981231)37:24<3397::aid-anie3397>3.0.co;2-n
Subject(s) - cytochrome c oxidase , chemistry , heme , cytochrome , ligand (biochemistry) , heme a , oxidase test , stereochemistry , oxidation reduction , biochemistry , enzyme , receptor
The environment of the Cu I ion in the distal ligand group decides the fate of the reduction of O 2 by the two analogues 1 and 2 of the heme a 3 Cu B center in cytochrome c oxidase. The fourfold coordination by N in 1 favors the Cu II oxidation state and leads to a 4 e − –4 H + reduction and the formation of H 2 O under physiological conditions, while with 2 a 2 e − –2 H + reduction occurs to form the cytotoxic H 2 O 2 .