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  • Title: Observation of the FeIV=O stretching vibration of ferryl myoglobin by resonance Raman spectroscopy.
    Author: Sitter AJ, Reczek CM, Terner J.
    Journal: Biochim Biophys Acta; 1985 Apr 29; 828(3):229-35. PubMed ID: 3986209.
    Abstract:
    We have directly observed the oxyferryl group of ferryl myoglobin by resonance Raman spectroscopy. The FeIV = O stretching vibration is observed at 797 cm-1 and confirmed by an 18O-induced isotopic shift to 771 cm-1. The porphyrin center-to-nitrogen distance of ferryl myoglobin is significantly less than that previously observed for horseradish peroxidase compound II, which also contains an FeIV = O heme. The FeIII-CN- stretch of myoglobin (FeIII) cyanide is observed at 454 cm-1, which shifts to 449 cm-1 upon substitution with [13C]cyanide.
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