Heme-Cu complexes as oxygen-activating functional models for the active site of cytochrome c oxidase

Yoshinori Naruta, Takao Sasaki, Fumito Tani, Yoishimitsu Tachi, Nobuo Kawato, Nobuhumi Nakamura

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44 Citations (Scopus)

Abstract

Tri(2-pyridylmethyl)amineCu complex-linked iron meso-tetraphenylporphyine derivatives were prepared to model the active site of cytochrome c oxidase. Exposure to oxygen converted the reduced forms of the complexes to the corresponding stable μ-peroxo species in spite of the presence of three coordination sites, two on the heme and one on the Cu. The oxy forms were characterized spectroscopically. Kinetic analyses of the oxygenation reactions of the reduced forms suggests that preferential O2 binding occurs at the Cu site over the heme. This mechanism is also supported by examination of the redox potentials of the two metal ions. Since the peroxy complexes of the models exhibit a structure similar to that of the previously reported fully-oxidized form, the relevance of the model chemistry to the enzyme reaction is discussed.

Original languageEnglish
Pages (from-to)239-246
Number of pages8
JournalJournal of inorganic biochemistry
Volume83
Issue number4
DOIs
Publication statusPublished - Jan 1 2001

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Inorganic Chemistry

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