Enhanced Reactivities of Iron(IV)‐Oxo Porphyrin Species in Oxidation Reactions Promoted by Intramolecular Hydrogen‐Bonding

Abstract High‐valent iron‐oxo species are one of the common intermediates in both biological and biomimetic catalytic oxidation reactions. Recently, hydrogen‐bonding (H‐bonding) has been proved to be critical in determining the selectivity and reactivity. However, few examples have been established for mechanistic insights into the H‐bonding effect. Moreover, intramolecular H‐bonding effect on both C‐H activation and oxygen atom transfer (OAT) reactions in synthetic porphyrin model system has not been investigated yet. In this study, a series of heme‐containing iron(IV)‐oxo porphyrin species with or without intramolecular H‐bonding are synthesized and characterized. Kinetic studies revealed that intramolecular H‐bonding can significantly enhance the reactivity of iron(IV)‐oxo species in OAT, C‐H activation, and electron‐transfer reactions. This unprecedented unified H‐bonding effect is elucidated by theoretical calculations, which showed that intramolecular H‐bonding interactions lower the energy of the anti‐bonding orbital of iron(IV)‐oxo porphyrin species, resulting in the enhanced reactivities in oxidation reactions irrespective of the reaction type. To the best of the knowledge, this is the first extensive investigation on the intramolecular H‐bonding effect in heme system. The results show that H‐bonding interactions have a unified effect with iron(IV)‐oxo porphyrin species in all three investigated reactions.