Add time:07/18/2019         Source:sciencedirect.com

Resonance Raman spectra of proto-, meso-, and deuteroheme (cas 18922-88-8)s isolated in cytochrome b5 have been recorded and effects due to sidegroup substituents noted. A one-to-one correspondence can be made between the fundamental Raman bands of mesoheme and deuteroheme, enabling identification of inductive effects on the porphyrin vibrations. (The saturated sidegroups of mesoheme produce Raman spectra very similar to cytochrome c.) Raman spectra of protoheme show extra structure which is produced by a resonance interaction between the vinyl sidegroups and deuteroheme core. Based on the resonance Raman data of protoheme it is possible to say that the red-shift in the absorption bands is due to extension of conjugation from the ring to the sidegroups rather than inductive effects of the sidegroups on the ring molecular orbitals.

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