Table 1. Comparison of peaks in Raman spectra of the whole heart, reduced or oxydized purified cytochrome c and purified oxy-or deoxymyoglobin.

Heart			Cytochrome c		Myoglobin		Comments
Control*	+SDT*	Contribution from**	Cyt.c(Fe 3+)	Cyt. c(Fe 2+)	dMb	oMb
—	604	cyts.c,c1(Fe2+)	—	604	—	—	Unique peak of cyts.c,c1(Fe2+)
750	750 ↑	cyts.c,c1(Fe2+), cyts.b(Fe2+)	750	750 ↑	750	—	SDT-induced increase of the peak intensity is a signature of cyts.
1127	1127 ↑	cyts.b(Fe2+), cyts.c (Fe2+)	1127	1127 ↑	—
1300–1310	1300–1310 ↑	cyts.c,c1,b(Fe2+)	1313	1313	—	—	In cyts.b the peak maximum locates at 1300 cm−1 [25]
1337	1337 ↑	cyts.b(Fe2+)	—	—	—	—	Unique peak of cyts.b(Fe2+)
—	1358(a)	dMb	—	—	1358(a)	—	Ratio of peak intensities at 1358 and 1377 cm−1 can be used to estimate relative dMb amount.
1377(a)	—	oMb	—	—	—	1377(a)
	1556(b)	dMb, oMb	—	—	1556(b) ↑	1556(b)	In heart under control conditions the spectrum range 1550–1640 cm−1 originates from oMb, whereas under SDT-reduction — from reduced cytochromes (1582 cm−1) and dMb (1556 and 1606 cm−1)
—	1582	cyts.c,c1,b(Fe2+)	1582	1582 ↑	—	—
1587(b)	—	oMb, dMb	—	—	1587(b)	1587(b) ↑
—	1606(c)	dMb	—	—	1606(c)	—
1640(c)	—	oMb	1638	—	—	1640(c)

^*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.