Resonance Raman spectra of hemoglobin and cytochrome c: inverse polarization and vibronic scattering.

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 degrees for 90 degrees 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, A(20), 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.