Magnetic circular dichroism studies on the heme and tryptophan components of cytochrome c peroxidase.

We have measured the magnetic circular dichroism of cytochrome c peroxidase and some of its derivatives from 250-350 nm. Comparison of the changes observed on conversion to the catalytic intermediate (cytochrome c peroxidase-I) with spectra obtained from horseradish peroxidase and its derivatives and model compounds of protoheme leads us to the conclusion that the observed changes in the magnetic circular dichroism spectra reflect conversion of the heme to the ferryl state. No evidence was found for modification of tryptophan in cytochrome c peroxidase-I.