Absorption spectra of cytochrome P450CAM in the reaction with peroxy acids

The reaction of Fe(III) cytochrome P450CAM with m-chloroperbenzoic acid was studied by rapid scanning absorption spectroscopy. Native low-spin enzyme produced spectra characteristic of two reaction phases that were marked by time intervals with isosbestic positions. The high-spin enzyme substrate complex yielded a series of Soret-region spectra whose properties were dependent on peracid concentration. The simplest model describing the results was a sequence of at least two spectral intermediates, that were not entirely homologous with data measured in reactions with microsomal P450LM2. Comparisons with related heme protein states indicate higher Fe(IV) oxidation levels provide a plausible interpretation of the P450CAM spectra.