A functional model of cytochrome c oxidase: Thermodynamic implications

James P. Collman*, Lei Fu, Paul C. Herrmann, Zhong Wang, Miroslav Rapta, Martin Bröring, Reinhold Schwenninger, Bernard Boitrel

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

64 Citations (Scopus)

Abstract

The environment of the Cu(I) ion in the distal ligand group decides the fate of the reduction of O2 by the two analogues 1 and 2 of the heme a3Cu(B) center in cytochrome c oxidase. The fourfold coordination by N in 1 favors the Cu(II) oxidation state and leads to a 4e--4H+ reduction and the formation of H2O under physiological conditions, while with 2 a 2e--2H+ reduction occurs to form the cytotoxic H2O2.

Original languageEnglish
Pages (from-to)3397-3400
Number of pages4
JournalAngewandte Chemie - International Edition
Volume37
Issue number24
DOIs
Publication statusPublished - 4 Jan 1999
Externally publishedYes

Keywords

  • Cytochrome c oxidase
  • Electrochemistry
  • Heme proteins
  • N ligands
  • O-O activation

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