DEVELOPMENT OF SUPRAMOLECULAR METALLOPROTEIN MIMICS

Supramolecular mimics of metalloproteins, viz. cytochrome P-450 and ir on-sulfur proteins are described. The cytochrome P-450 mimic consists of a Mn porphyrin and a Rh complex which are incorporated within a ves icle membrane in water. This system catalyses the reductive activation of molecular oxygen in the epoxidation of alkenes at Mn, with reducin g equivalents derived from the simultaneous Rh catalysed oxidation of formate to carbon dioxide. In the mimics for iron-sulfur proteins, iro n-sulfur clusters are encapsulated in diphenylglycoluril and cyclotriv eratrylene cavitands. The encapsulation by the cavitands modifies the electrochemical parameters, e.g. the redox potential, of the iron-sulf ur clusters, in a way that has certain analogies to the effects of enc apsulation by the protein in ferredoxins and high-potential iron-sulfu r proteins.