A functional model of the cytochrome c oxidase active site: Unique conversion of a heme-μ-peroxo-CuII intermediate into heme-superoxo/CuI

Jin Gang Liu, Yoshinori Naruta, Fumito Tani

Research output: Contribution to journalArticlepeer-review

67 Citations (Scopus)

Abstract

(Chemical Equation Presented) Axial ligation of the heme moiety by a proximal imidazole group is observed in a novel cytochromec oxidase (CcO) active-site model 1 in which the copper ion is bound to a N-(2-hydroxyphenyl) imidazole moiety. Spectroscopic observations of 1 suggest the unique transformation of an initial heme-μ-peroxo-CuII species into a heme-superoxide/CuI intermediate in the course of the CcO oxygenation reaction at low temperature.

Original languageEnglish
Pages (from-to)1836-1840
Number of pages5
JournalAngewandte Chemie - International Edition
Volume44
Issue number12
DOIs
Publication statusPublished - Mar 11 2005

All Science Journal Classification (ASJC) codes

  • Catalysis
  • Chemistry(all)

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