Abstract
Resonance Raman spectra have been obtained for Compound II of horseradish peroxidase. Its prophyrin vibrational frequencies are consistent with a planar low-spin heme containing Fe(IV). The oxidation-state marker band is found at the unprecedentedly high value of 1382 cm −1. This band was also observed in solutions of myoglobin and cytochrome c peroxidase to which H 2O 2 had been added. No evidence was found for an actual FeO double bond in Compound II.
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