Investigations of the resonance Raman excitation profiles of cytochrome

O. Bangcharoenpaurpong, P. M. Champion, Susan A. Martinis, Stephen G. Sligar

Research output: Contribution to journalArticlepeer-review


We have measured the resonance Raman excitation profiles (REP's) of several vibrational modes associated with the heme active site of cytochrome P 450 cam. The important Fe-S axial ligand mode (351 cm-1) of the substrate bound (high-spin ferric) complex is found to have structure in its blue shifted REP. Inverse transform techniques allow the line shape of the resonant charge transfer absorption to be reconstructed directly from the REP data. The observed splitting (3200 cm-1) is associated with an inequivalence in the resonant S→Fe charge transfer excitations. The position of the high-energy component (∼323 nm) is found to be in excellent agreement with z-polarized single crystal measurements, while the low-energy component (∼360 nm) is not clearly observed in the single crystal analysis. The "spin-marker" band ν3 is found to have a REP that is significantly red shifted with respect to the theoretical predictions. A variety of perturbations including non-Condon and multiple state coupling, as well as state dependent damping, are unable to account for the observed red shift. Studies of other ferric heme protein systems, including substrate free cytochrome P 450cam, (low-spin) and aquomet myoglobin (high-spin) reveal "normal" behavior of their REP's. The electron-nuclear coupling strengths are directly extracted from the measured absolute cross sections in these cases.

Original languageEnglish (US)
Pages (from-to)4273-4284
Number of pages12
JournalThe Journal of Chemical Physics
Issue number8
StatePublished - 1987

ASJC Scopus subject areas

  • Physics and Astronomy(all)
  • Physical and Theoretical Chemistry


Dive into the research topics of 'Investigations of the resonance Raman excitation profiles of cytochrome'. Together they form a unique fingerprint.

Cite this