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

Research output: Contribution to journalArticle

32 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 languageEnglish
Pages (from-to)120-121
Number of pages2
JournalChemical Communications
Volume4
Issue number1
DOIs
Publication statusPublished - Jan 1 2004

Fingerprint

Electron Transport Complex IV
Heme
Histidine
Tyrosine
Copper
Oxygen
Porphyrins
Phenol
Phenols
Iron
imidazole

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

Cite this

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; Chishiro, Takefumi; Tachi, Yoshimitsu.

In: Chemical Communications, Vol. 4, No. 1, 01.01.2004, p. 120-121.

Research output: Contribution to journalArticle

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