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Resonance Raman Spectra Of Chloroperoxidase Reaction Intermediates, Ann Marie G. Sullivan
Resonance Raman Spectra Of Chloroperoxidase Reaction Intermediates, Ann Marie G. Sullivan
Theses and Dissertations
Chloroperoxidase is an enzyme that exhibits spectroscopic and structural properties similar to cytochrome P-450. Chloroperoxidase is studied using resonance Raman spectroscopy to characterize the reaction intermediates of the physiological mechanism, known as compounds I and II. Compound I is formed by a two electron oxidation of the resting enzyme and contains an Fe(IV) porphyrin ℼ cation radical. A one electron reduction of compound I produces the compound II intermediate which contains an oxy-ferryl [Fe(IV)=O] iron heme.
Chloroperoxidase is a heme enzyme of substantial interest because of its structural similarity to cytochrome P-450 and because of its diverse reactivity. Chloroperoxidase can …