Meso-unsubstituted iron corrole in hemoproteins: remarkable differences in effects on peroxidase activities between myoglobin and horseradish peroxidase

Myoglobin (Mb) and horseradish peroxidase (HRP) are both reconstituted with a meso-unsubstituted iron corrole and their electronic configurations and peroxidase activities are examined. The catalytic activities of both proteins toward guaiacol oxidation are different and this finding is attributed to the difference in the oxidation states of the corrole iron when these proteins are in the resting state.