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

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

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
Volume579
Issue number28
DOIs
StatePublished - Nov 21 2005

Fingerprint

Oxygen Isotopes
Raman Spectrum Analysis
Electron Transport Complex IV
Carbon Monoxide
Isotopes
Raman spectroscopy
Structural properties
Substitution reactions
Oxygen
Enzymes

Keywords

  • Bioenergetics
  • Biophysics
  • Ferryl
  • Proton pumping
  • Raman

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Structural characterization of the PCO/O2 compound of cytochrome c oxidase. / Ji, Hong; Yeh, Syun-Ru; Rousseau, Denis L.

In: FEBS Letters, Vol. 579, No. 28, 21.11.2005, p. 6361-6364.

Research output: Contribution to journalArticle

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