Observation of the FeIV=O stretching vibration of ferryl myoglobin by resonance Raman spectroscopy.
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.
D000818:Animals; D003486:Cyanides; D006735:Horseradish Peroxidase; D007501:Iron; D009211:Myoglobin; D010103:Oxygen Isotopes; D013059:Spectrum Analysis, Raman; D014732:Vibration
D003486:Cyanides; D009211:Myoglobin; D010103:Oxygen Isotopes; D007501:Iron; D006735:Horseradish Peroxidase