Mechanistic Insight into Formation of Oxo‐Iron(IV) Porphyrin π‐Cation Radicals from Enzyme Mimics of Cytochrome P450 in Organic Solvents

Two new models for cytochrome P450 in which the thiolate axial ligand is replaced by an RSO 3 − group, form oxo‐iron(IV) porphyrin π‐cation radicals as sole oxidation products in “peroxo shunt” reactions (see scheme) independent of the nature of the employed solvent (polar or non‐polar) and electronic nature of the porphyrin rings.Two new models for cytochrome P450 in which the thiolate axial ligand is replaced by a RSO 3 − group, form oxo‐iron(IV) porphyrin π‐cation radicals as sole oxidation products in “peroxo shunt” reactions independent of the nature of the employed solvent (polar or non‐polar) and electronic nature of the porphyrin rings. Although the properties of the solvent and push–pull effects from the porphyrin rings do not affect the mode of the OO bond cleavage (heterolytic or homolytic) in these models, they strongly affect the rate and mechanism of each reaction step leading to the formation of the high‐valent iron intermediates. This article reports the results of mechanistic studies involving the measurements of the rate of oxo‐iron(IV) porphyrin π‐cation radical formation from the enzyme mimics of P450 for different oxidant concentration, temperature and pressure in selected organic solvents. Extraction of the appropriate rate constants and activation parameters for the reactions studied enable a detailed discussion of the effects of solvent and electronic nature of the porphyrin rings on the position of the first pre‐equilibrium involving formation of the acylperoxo‐iron(III) porphyrin intermediate, as well as on the rate of heterolytic OO bond cleavage leading to the formation of the high‐valent iron species. Furthermore, an unusual effect of solvent on the kinetics of oxo‐iron(IV) porphyrin π‐cation radical formation in methanol is demonstrated and discussed in the present work.