Structural characterization of the PCO/O2 compound of cytochrome c oxidase

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4 Scopus citations


The structural properties of a key transient oxygen intermediate of cytochrome c oxidase, PR, remain an enigma, although inferences have been drawn from its equilibrium analogues, PCO/O2, PH and P M. With resonance Raman spectroscopy, an oxygen isotope-sensitive band at 806 cm-1 was observed in PCO/O2 produced by adding CO and O2 to the resting enzyme. The vibrational band shifted to 771 cm -1 upon isotopic substitution of 16O2 with 18O2. The same modes at 806 and 771 cm-1 were present simultaneously when the mixed isotope, 18O16O, was employed, indicating that in PCO/O2 the O-O bond is cleaved, resulting in a Fe4+O2- structure. This result unifies the nature of the three equilibrium analogues of the PR intermediate.

Original languageEnglish (US)
Pages (from-to)6361-6364
Number of pages4
JournalFEBS Letters
Issue number28
StatePublished - Nov 21 2005


  • Bioenergetics
  • Biophysics
  • Ferryl
  • Proton pumping
  • Raman

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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