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

Literature Information

Publication Date 2003-11-24
DOI 10.1039/B311538K
Impact Factor 6.222
Authors

Jin-Gang Liu, Yoshinori Naruta, Fumito Tani, Takefumi Chishiro, Yoshimitsu Tachi


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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.

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Chemical Communications

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ChemComm publishes urgent research which is of outstanding significance and interest to experts in the field, while also appealing to the journal’s broad chemistry readership. Our communication format is ideally suited to short, urgent studies that are of such importance that they require accelerated publication. Our scope covers all topics in chemistry, and research at the interface of chemistry and other disciplines (such as materials science, nanoscience, physics, engineering and biology) where there is a significant novelty in the chemistry aspects. Major topic areas covered include: Analytical Chemistry Catalysis Chemical Biology and medicinal chemistry Computational Chemistry and Machine Learning Energy and sustainable chemistry Environmental Chemistry Green Chemistry Inorganic Chemistry Materials Chemistry Nanoscience Organic Chemistry Physical Chemistry Polymer Chemistry Supramolecular Chemistry

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