Table 1. Positions and assignments of bands in Raman spectra of cardiomyocytes.^* .

Frequency, cm−1	Bond in heme molecule*	Symmetry of vibration*	Sensitivity of vibration*	Hemoprotein*	Main contribution from**
747–750	heme breathing	B1g, 15	Redox state of heme Fe,	cytochromes , , , , , oMb	cytochromes ,
1125		B1g, 5	Redox state of cytochromes , ,	cytochromes , , , , , oMb	cytochromes , ,
1170	asymmetric pyrrol half-ring	B2g, 30	Redox state of heme Fe,	cytochromes , , , , , oMb	cytochromes , , , ,
1297	all heme bonds	21	Redox and spin state of heme Fe, presence of O2	oMb	oMb
1301–1305	all heme bonds	21	Redox state of heme Fe,	cytochromes , , , ,	cytochromes , , , ,
1335	all heme bond		Redox state of heme Fe,	cytochromes , , , ,	cytochromes , , , ,
1370–1375	symmetric pyrrol half-ring	A1g, 4	Redox state of heme Fe, presence of O2	oMb	oMb
1585	,	A2g	Redox and spin state of heme Fe, diameter of heme ring	cytochromes , , , , , oMb	cytochromes , , , , , oMb
1640	, ,	B1g, 10	Spin state of heme Fe, diameter of heme ring	oMb	oMb

^*Based on papers [11]–[13], [18], [35].

^**Based on [12], [18] and our own observations. Frequencies indicated in bold type refer to the peaks discussed in the text.