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Examination of nickel(II) microperoxidase-11 (NiMP-11) was conducted via resonance Raman and ultraviolet-visible absorption spectra. The results showed that increase in heme distortion is caused by the peptide even after the removal of the rest of the protein and the Fe-histide linkage. Moreover, the results revealed that determination of the heme structure is attributed to the conformation of the fingerprint peptide, not merely to its presence, as shown by its H-dependent behavior.

Conformational differences in the hemes in ferricytochromes c(sub3) have been investigated using resonance Raman spectroscopy, molecular mechanics calculations and normal-coordinate structural decomposition techniques. The observed nonplanarity is mainly due to a fingerprint peptide segment, and factors influencing the folding pattern of the fingerprint peptide and other peptide-heme contacts also have an effect on heme conformation.

A study was conducted to examine the effects of proteins on the nonplanarity of the macrocycle in nickel cytochrome c using molecular mechanics computations and resonance Raman spectroscopy. A dual-channel spectrometer was utilized to determine RR spectra while the POLYGRAF software was used to perform molecular mechanics computations. Results indicated that the nonplanar distortion of the porphyrin of cytochromes c is supported by a small protein segment.