Comparison of peaks in Raman spectra of the whole heart, reduced or oxydized purified cytochrome c and purified oxy-or deoxymyoglobin.

*The same set of peaks we observe in Raman spectra of cardiomyocytes and isolated CM mitochondria;
**Based on [11], [16], [17], [25] and our own observations;
(a)— symmetric pyrrol half-ring vibrations of Mb heme (A1g/4 symmetry), sensitive to the Redox state of heme Fe and presence of O2;
(b)and(c)— vibrations of heme methine-bridges (A1g and B1g/10 symmetry, respectively), sensitive to the spin state of heme Fe and diameter of the heme ring.
Numbers indicate positions of peak maxima (cm−1). Arrows mark peaks whose intensity significantly increases in Raman spectra of the heart after SDT application, reduction of cytochrome c, or under binding or release of O2 from myoglobin. Cytochrome or Mb type indicated in bold font is the main contributer to the Raman scattering of the heart at the designated frequency shift.