A FUNCTIONAL MIMIC OF NATURAL PEROXIDASES - SYNTHESIS AND CATALYTIC ACTIVITY OF A NONHEME IRON PEPTIDE HYDROPEROXIDE COMPLEX

Site-selective attachment of unprotected peptides to a non-heme iron c omplex is achieved by displacing two halides on the catalyst by peptid e caesium thiolates, This coupling approach should be compatible with any peptide sequence provided there is only a single reduced cysteine. The oxidation activity with hydrogen peroxide of the dipeptide-cataly st complex in water is retained, and shows similarities with oxidation mechanisms observed for natural oxidizing enzymes, The results pave t he way for the future design of peroxidase mimics where the activity o f the catalyst will be modulated by a designed protein matrix.