Coordination structure and chemical reactivity of hemoprotein-butyl peroxide complex

ESR and optical spectra ascribed to be the hemoprotein-butylperoxide complex were detected for the frozen aqueous solution containing whale met-Mb and t- or n-butylhydroperoxide at pH 10. The observed ESR and optical parameters of the complex were characteristic to those of six coordinate ferric low-spin complexes, having the butylperoxide anion at the axial position of heme. pH dependent ESR measurements demonstrated the formation of the complex in the biological pH regions (7.0). Time dependent ESR and optical measurements indicated that the complex may be one of the intermediate species in the processes of heme degradation reaction induced by butylperoxide.