Skip to main content
NCBI home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1972 Sep;69(9):2622–2626. doi: 10.1073/pnas.69.9.2622

Resonance Raman Spectra of Hemoglobin and Cytochrome c: Inverse Polarization and Vibronic Scattering

Thomas G Spiro 1, Thomas C Strekas 1
PMCID: PMC427002  PMID: 4506783

Abstract

Resonance Raman spectra of hemoglobin and cytochrome c in dilute solution contain prominent bands that exhibit inverse polarization, i.e., the polarization vector of the incident radiation is rotated through 90° for 90° scattering, giving infinite depolarization ratios. This phenomenon is shown to require an antisymmetric molecular-scattering tensor. The antisymmetry, which is characteristic of resonance scattering, is associated with the form of a particular class of vibrations, A20, of the tetragonal heme chromophores. The dependence of the resonance Raman spectra on the wavelength of the exciting radiation, as well as their polarization properties, demonstrates that the prominent bands correspond to vibronically active modes of the first electronic transition of the heme proteins, and provide confirmation of Albrecht's vibronic theory of Raman intensities.

Keywords: scattering tensor, porphyrin fluorescence

Full text

PDF
2622

Selected References

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

  1. Dickerson R. E., Takano T., Eisenberg D., Kallai O. B., Samson L., Cooper A., Margoliash E. Ferricytochrome c. I. General features of the horse and bonito proteins at 2.8 A resolution. J Biol Chem. 1971 Mar 10;246(5):1511–1535. [PubMed] [Google Scholar]
  2. Eaton W. A., Hochstrasser R. M. Electronic spectrum of single crystals of ferricytochrome-c. J Chem Phys. 1967 Apr 1;46(7):2533–2539. doi: 10.1063/1.1841081. [DOI] [PubMed] [Google Scholar]
  3. MARGOLIASH E., FROHWIRT N. Spectrum of horse-heart cytochrome c. Biochem J. 1959 Mar;71(3):570–572. doi: 10.1042/bj0710570. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Perutz M. F., Muirhead H., Cox J. M., Goaman L. C. Three-dimensional Fourier synthesis of horse oxyhaemoglobin at 2.8 A resolution: the atomic model. Nature. 1968 Jul 13;219(5150):131–139. doi: 10.1038/219131a0. [DOI] [PubMed] [Google Scholar]
  5. Salmeen I., Palmer G. Electron paramagnetic resonance of beef-heart ferricytochrome c. J Chem Phys. 1968 Mar 1;48(5):2049–2052. doi: 10.1063/1.1669014. [DOI] [PubMed] [Google Scholar]
  6. Strekas T. C., Spiro T. G. Cytochrome c: resonance Raman spectra. Biochim Biophys Acta. 1972 Aug 31;278(1):188–192. doi: 10.1016/0005-2795(72)90121-3. [DOI] [PubMed] [Google Scholar]
  7. Strekas T. C., Spiro T. G. Hemoglobin: resonance Raman spectra. Biochim Biophys Acta. 1972 May 18;263(3):830–833. doi: 10.1016/0005-2795(72)90072-4. [DOI] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES