A comprehensive test set of epoxidation rate constants for iron(iv)-oxo porphyrin cation radical complexes.

ABSTRACT: Cytochrome P450 enzymes are heme based monoxygenases that catalyse a range of oxygen atom transfer reactions with various substrates, including aliphatic and aromatic hydroxylation as well as epoxidation reactions. The active species is short-lived and difficult to trap and characterize experimentally, moreover, it reacts in a regioselective manner with substrates leading to aliphatic hydroxylation and epoxidation products, but the origin of this regioselectivity is poorly understood. We have synthesized a model complex and studied it with low-pressure Fourier transform-ion cyclotron resonance (FT-ICR) mass spectrometry (MS). A novel approach was devised using the reaction of [Fe^III(TPFPP)]⁺ (TPFPP = meso-tetrakis(pentafluorophenyl)porphinato dianion) with iodo

SUBMITTER: Sainna MA 

PROVIDER: S-EPMC5811088 | biostudies-literature | 2015 Feb

REPOSITORIES: biostudies-literature