Vibrational structure of the formyl group on heme a: Implications on the properties of cytochrome c oxidase

S. Han, Y. C. Ching, S. L. Hammes, Denis L. Rousseau

Research output: Contribution to journalArticle

21 Citations (Scopus)

Abstract

Resonance Raman spectra have been recorded for heme a derivatives in which the oxygen atom of the formyl group has been isotopically labeled and for Schiff base derivatives of heme a in which the Schiff base nitrogen has been isotopically labeled. The 14N-15N isotope shift in the C==N stretching mode of the Schiff base is close to the theoretically predicted shift for an isolated C==N group for both the ferric and ferrous oxidation states and in both aqueous and nonaqueous solutions. In contrast, the 16O-18O isotope shift of the C==O stretching mode of the formyl group is significantly smaller than that predicted for an isolated C==O group and is also dependent on whether the environment is aqueous or nonaqueous. This differences between the theoretically predicted shifts and the observed shifts are attributed to coupling of the C==O stretching mode to as yet unidentified modes of the heme. The complex behavior of the C==O stretching vibration precludes the possibility of making simple interpretations of frequency shifts of this mode in cytochrome c oxidase.

Original languageEnglish (US)
Pages (from-to)45-52
Number of pages8
JournalBiophysical Journal
Volume60
Issue number1
StatePublished - 1991
Externally publishedYes

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Schiff Bases
Electron Transport Complex IV
Isotopes
Vibration
Heme
Nitrogen
Oxygen
heme a

ASJC Scopus subject areas

  • Biophysics

Cite this

Vibrational structure of the formyl group on heme a : Implications on the properties of cytochrome c oxidase. / Han, S.; Ching, Y. C.; Hammes, S. L.; Rousseau, Denis L.

In: Biophysical Journal, Vol. 60, No. 1, 1991, p. 45-52.

Research output: Contribution to journalArticle

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AU - Rousseau, Denis L.

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