A Functional Model of the Cytochrome  c  Oxidase Active Site: Unique Conversion of a Heme–μ‐peroxo–Cu II  Intermediate into Heme– superoxo/Cu I | Zendy

Liu JinGang | Zendy; Naruta Yoshinori | Zendy; Tani Fumito | Zendy

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A Functional Model of the Cytochrome c Oxidase Active Site: Unique Conversion of a Heme–μ‐peroxo–Cu II Intermediate into Heme– superoxo/Cu I

Author(s) -

Liu JinGang,

Naruta Yoshinori,

Tani Fumito

Publication year - 2005

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/anie.200462582

Subject(s) - moiety , heme , imidazole , chemistry , cytochrome c oxidase , heme a , cytochrome , active site , stereochemistry , oxidase test , hemeprotein , photochemistry , catalysis , enzyme , biochemistry

Axial ligation of the heme moiety by a proximal imidazole group is observed in a novel cytochrome c oxidase (C c O) active‐site model 1 in which the copper ion is bound to a N ‐(2‐hydroxyphenyl)imidazole moiety. Spectroscopic observations of 1 suggest the unique transformation of an initial heme–μ‐peroxo–Cu II species into a heme–superoxide/Cu I intermediate in the course of the C c O oxygenation reaction at low temperature.

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