THE ACTIVE SITE OF THE ENZYME P-450 MONOOXYGENASE IS AN IRON PORPHYRIN SURROUNDED BY PROTEINS WHICH CAN SELECTIVELY CATALYZES THE A WIDE RANGE OF REACTIONS INCLUDING OXYGEN TRANSFER TO HETEROATOMS, EPOXIDATION OF OLEFINS, HYDROXYLATION OF AROMATIC HYDROCARBONS AND OXIDATIVE DEGRADATION OF CHEMICALLY INERT XENOBIOTICS SUCH AS DRUGS AND ENVIRONMENTAL CONTAMINANTS [1]. IN ORDER TO UNDERSTAND THE MECHANISM OF CYTOCHROME P-450 MONOOXYGENATION ENZYME, SYNTHETIC METALLOPORPHYRINS HAVE BEEN USED AS CYTOCHROME P-450 MODELS [2]. DESPITE SEVERAL REPORTS ON THE APPLICATIONS OF METALLOPORPHYRINS IN THE OXIDATION OF ORGANIC COMPOUNDS, THERE ARE FEW REPORTS ON THEIR APPLICATIONS AS Lewis ACID CATALYSTS. HIGH-VALENT METALLOPORPHYRINS, IN WHICH THE METAL IS IN ITS HIGHEST OXIDATION STATE, CAN BE USED AS MILD Lewis ACIDS. IN THIS RESPECT, ELECTRON-DEFICIENT PORPHYRINS OF CR (III), FE (III), SN (IV) AND V (IV) HAVE BEEN USED IN ORGANIC TRANSFORMATIONS SUCH AS REGIOSELECTIVE [3, 3] REARRANGEMENT OF ALIPHATIC ALLYL VINYL ETHERS, CLAISEN REARRANGEMENT OF SIMPLE ALIPHATIC ALLYL VINYL ETHERS, REARRANGEMENT OF A, B-EPOXY KETONES INTO 1, 2-DIKETONES, REARRANGEMENT OF MONOALKYLSUBSTITUTED EPOXIDES INTO ALDEHYDES, HIGHLY REGIO- AND STEREOSELECTIVE REARRANGEMENT OF EPOXIDES TO ALDEHYDES, EPOXIDE RING-OPENING, PROTECTION OF HYDROXYL COMPOUNDS, CYCLOPROPANATION OF ALKENES, OLEFIN FORMATION AND CO2 FIXATION [3-10].