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

Jin Gang Liu; Yoshinori Naruta; Fumito Tani; Takefumi Chishiro; Yoshimitsu Tachi

doi:10.1039/b311538k

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

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

Department of Applied Molecular Chemistry

Research output: Contribution to journal › Article › peer-review

37 Citations (Scopus)

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.

Original language	English
Pages (from-to)	120-121
Number of pages	2
Journal	Chemical Communications
Volume	4
Issue number	1
DOIs	https://doi.org/10.1039/b311538k
Publication status	Published - 2004

All Science Journal Classification (ASJC) codes

Catalysis
Electronic, Optical and Magnetic Materials
Ceramics and Composites
Chemistry(all)
Surfaces, Coatings and Films
Metals and Alloys
Materials Chemistry

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10.1039/b311538k

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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. / Liu, Jin Gang; Naruta, Yoshinori; Tani, Fumito et al.
In: Chemical Communications, Vol. 4, No. 1, 2004, p. 120-121.

Research output: Contribution to journal › Article › peer-review

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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

Abstract

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