Skip to main content
Biophysical Journal logoLink to Biophysical Journal
. 1991 Jul;60(1):45–52. doi: 10.1016/S0006-3495(91)82029-X

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

S W Han 1, Y C Ching 1, S L Hammes 1, D L Rousseau 1
PMCID: PMC1260037  PMID: 1653051

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.

Full text

PDF
45

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Babcock G. T., Callahan P. M., Ondrias M. R., Salmeen I. Coordination geometries and vibrational properties of cytochromes alpha and alpha 3 in cytochrome oxidase from Soret excitation Raman spectroscopy. Biochemistry. 1981 Feb 17;20(4):959–966. doi: 10.1021/bi00507a049. [DOI] [PubMed] [Google Scholar]
  2. Babcock G. T., Callahan P. M. Redox-linked hydrogen bond strength changes in cytochrome a: implications for a cytochrome oxidase proton pump. Biochemistry. 1983 May 10;22(10):2314–2319. doi: 10.1021/bi00279a002. [DOI] [PubMed] [Google Scholar]
  3. Callahan P. M., Babcock G. T. Origin of the cytochrome a absorption red shift: a pH-dependent interaction between its heme a formyl and protein in cytochrome oxidase. Biochemistry. 1983 Jan 18;22(2):452–461. doi: 10.1021/bi00271a031. [DOI] [PubMed] [Google Scholar]
  4. Caughey W. S., Smythe G. A., O'Keeffe D. H., Maskasky J. E., Smith M. I. Heme A of cytochrome c oxicase. Structure and properties: comparisons with hemes B, C, and S and derivatives. J Biol Chem. 1975 Oct 10;250(19):7602–7622. [PubMed] [Google Scholar]
  5. Ching Y. C., Argade P. V., Rousseau D. L. Resonance raman spectra of CN--bound cytochrome oxidase: spectral isolation of cytochromes a2+, a3(2+), and a3(2+)(CN-). Biochemistry. 1985 Aug 27;24(18):4938–4946. doi: 10.1021/bi00339a032. [DOI] [PubMed] [Google Scholar]
  6. Ondrias M. R., Babcock G. T. Resonance enhancement of the vibrations of cytochrome -a3 and its conformation in oxidized cytochrome oxidase. Biochem Biophys Res Commun. 1980 Mar 13;93(1):29–35. doi: 10.1016/s0006-291x(80)80241-5. [DOI] [PubMed] [Google Scholar]
  7. Rousseau D. L., Ondrias M. R., LaMar G. N., Kong S. B., Smith K. M. Resonance Raman spectra of the heme in leghemoglobin. Evidence for the absence of ruffling and the influence of the vinyl groups. J Biol Chem. 1983 Feb 10;258(3):1740–1746. [PubMed] [Google Scholar]
  8. Salmeen I., Rimai L., Babcock G. Raman spectra of heme a, cytochrome oxidase-ligand complexes, and alkaline denatured oxidase. Biochemistry. 1978 Mar 7;17(5):800–806. doi: 10.1021/bi00598a008. [DOI] [PubMed] [Google Scholar]
  9. Salmeen I., Rimai L., Gill D., Yamamoto T., Palmer G., Hartzell C. R., Beinert H. Resonance Raman spectroscopy of cytochrome c oxidase and electron transport particles with excitation near the Soret band. Biochem Biophys Res Commun. 1973 Jun 8;52(3):1100–1107. doi: 10.1016/0006-291x(73)91051-6. [DOI] [PubMed] [Google Scholar]
  10. Sassaroli M., Ching Y. C., Dasgupta S., Rousseau D. L. Cytochrome c oxidase: evidence for interaction of water molecules with cytochrome a. Biochemistry. 1989 Apr 18;28(8):3128–3132. doi: 10.1021/bi00434a002. [DOI] [PubMed] [Google Scholar]
  11. TAKEMORI S., KING T. E. EFFECT OF ALKALI AND BOROHYDRIDE ON CARDIAC CYTOCHROME OXIDASE. FORMATION OF SCHIFF BASE. J Biol Chem. 1965 Jan;240:504–513. [PubMed] [Google Scholar]
  12. Tsubaki M., Nagai K., Kitagawa T. Resonance Raman spectra of myoglobins reconstituted with spirographis and isospirographis hemes and iron 2,4-diformylprotoporphyrin IX. Effect of formyl substitution at the heme periphery. Biochemistry. 1980 Jan 22;19(2):379–385. doi: 10.1021/bi00543a020. [DOI] [PubMed] [Google Scholar]

Articles from Biophysical Journal are provided here courtesy of The Biophysical Society

RESOURCES