The peroxidases react with hydrogen peroxide to cleave the 0-0 bond and produce a protohemin derivative that is 2e-equiv more oxidized than the resting Fe (II1) p~ rphyrin.~,~ Recent evidence suggests that at least one of the electrons is removed from the porphyrin? r system to give a cation radical that is responsible for much of the electron transfer involved in substrate oxidation^.^^^
![4-[(10Z,14Z)-10,15-bis(3,5-ditert-butyl-4-hydroxyphenyl)-20-(3,5-ditert-butyl-4-oxocyclohexa-2,5-dien-1-ylidene)-21,22,23,24-tetrahydroporphyrin-5-ylidene]-2,6-ditert-butylcyclohexa-2,5-dien-1-one Structure](https://image.chemsrc.com/caspic/195/74684-36-9.png)