Catalytic activities of an artificial heme enzyme

Abstract

Heme proteins, which have an iron porphyrin at the active site, such as peroxidase and cytochrome P-450 catalyze various oxidation reactions efficiently. Hemes have been successfully introduced to polypeptides non-covalently [1] or covalently [2] so far. We also attempted to functionalize the de novo designed polypeptide, by introducing iron porphyrins. We utilized cysteine residues to combine synthetic porphyrin rings covalently via thioether linkages. In the present study, we demonstrate the peroxidase-like activity with an amphiphilic βαβαstructure with two iron porphyrins as an artificial heme enzyme.