Identification of heme propionate vibrational modes in the resonance Raman spectra of cytochrome c oxidase

Tsuyoshi Egawa, Hyun Ju Lee, Hong Ji, Robert B. Gennis, Syun-Ru Yeh, Denis L. Rousseau

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

The propionate groups of heme a and a3 in cytochrome c oxidase (CcO) have been postulated to mediate both the electron and proton transfer within the enzyme. To establish structural markers for the propionate groups, their associated vibrational modes were identified in the resonance Raman spectra of CcO from bovine (bCcO) and Rhodobacter sphaeroides (RsCcO). The distinction between the modes from the propionates of heme a and heme a3, as well as those from the propionates on the pyrrole rings A and D in each heme, was made on the basis of H2O-D2O isotope substitution experiments combined with wavelength-selective resonance enhancement (for bCcO) or mutagenesis studies (for RsCcO).

Original languageEnglish (US)
Pages (from-to)141-143
Number of pages3
JournalAnalytical Biochemistry
Volume394
Issue number1
DOIs
StatePublished - Nov 1 2009

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Propionates
Electron Transport Complex IV
Heme
Raman scattering
Rhodobacter sphaeroides
Mutagenesis
Pyrroles
Proton transfer
Isotopes
Protons
Substitution reactions
Electrons
Wavelength
heme a
Enzymes
Experiments

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology
  • Cell Biology

Cite this

Identification of heme propionate vibrational modes in the resonance Raman spectra of cytochrome c oxidase. / Egawa, Tsuyoshi; Lee, Hyun Ju; Ji, Hong; Gennis, Robert B.; Yeh, Syun-Ru; Rousseau, Denis L.

In: Analytical Biochemistry, Vol. 394, No. 1, 01.11.2009, p. 141-143.

Research output: Contribution to journalArticle

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