Absorbance Fourier transform infrared (FTIR) spectra of model compounds for heme proteins such as protoporphyrin‐IX, hemin, and hematin have been directly compared to the data of electrochemically induced FTIR difference spectra of small c‐type proteins, i.e., microperoxidase‐11, and cytochrome c. A band at 840–830 cm−1 occurring in all studied samples dominated the spectra. The position of this vibrational mode depends on pH and the oxidation state, and could be assigned to the γ(CH) mode of the porphyrin ring. Further features, such as the ring vibrations sensitive for the presence of iron and its oxidation state, are shown in the low‐frequency infrared region between 750 and 650 cm−1. © 2006 Wiley Periodicals, Inc. Biopolymers 82:349–352, 2006 This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com
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Dörr et al. (2006) studied this question.