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Issue 1, 2004
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Formation and spectroscopic characterization of the dioxygen adduct of a heme–Cu complex possessing a cross-linked tyrosine–histidine mimic: modeling the active site of cytochrome c oxidase

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Abstract

A binucleating porphyrin with covalently appended copper chelates having a cross-linked imidazole–phenol group as the novel active site model of cytochrome c oxidase has been prepared, and the dioxygen adduct of its iron(II)–copper(I) complex was spectroscopically characterized.

Graphical abstract: Formation and spectroscopic characterization of the dioxygen adduct of a heme–Cu complex possessing a cross-linked tyrosine–histidine mimic: modeling the active site of cytochrome c oxidase

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Supplementary files

Article information


Submitted
19 Sep 2003
Accepted
21 Oct 2003
First published
24 Nov 2003

Chem. Commun., 2004, 120-121
Article type
Communication

Formation and spectroscopic characterization of the dioxygen adduct of a heme–Cu complex possessing a cross-linked tyrosine–histidine mimic: modeling the active site of cytochrome c oxidase

J. Liu, Y. Naruta, F. Tani, T. Chishiro and Y. Tachi, Chem. Commun., 2004, 120 DOI: 10.1039/B311538K

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