Description:
<jats:p> Dioxygen adducts of heme proteins are ubiquitous in all O<jats:sub>2</jats:sub> activating/reducing heme proteins in nature. While artificial dioxygen adducts of heme are known for six decades, till date these have not been demonstrated to be able to oxidize organic substrates in sharp contrast to their non-heme analogues and naturally occurring enzymes like heme dioxygenases. To address this apparent anomaly an iron porphyrin complex is synthesized which includes a pendant quinol group. The corresponding dioxygen bound iron porphyrin species is demonstrated to perform Hydrogen atom transfer (HAT) from a quinol group appended to the porphyrin ligand. The resultant ferric peroxide, formed by the first HAT, performs a 2<jats:sup>nd</jats:sup> HAT generating a ferryl species (Fe<jats:sup>IV</jats:sup>=O) and resulting in the 2e<jats:sup>-</jats:sup>/2H<jats:sup>+</jats:sup> oxidation of the pendant hydroquinol to quinone. All the intermediate species are trapped at cryogenic temperatures and spectroscopically characterized using EPR and resonance Raman spectroscopy. DFT calculations reproduce the experimental kinetic parameters and provide insight into the nature of TS involved. These results demonstrate that artificial analogues of both heme ferric superoxide and ferric hydroperoxide species can perform HAT from an organic substrate when appropriately pre-organized to hydrogen bond to the bound superoxide and peroxide species. Siilarly, catalytic oxidation of organic substrates, using a green oxidant like O<jats:sub>2</jats:sub>, has been a long-term goal of the scientific community. In nature, these oxidations are performed by metalloenzymes which generate highly oxidizing species from O<jats:sub>2</jats:sub> which, in turn, can oxidize inert organic substrates e.g. mono/di oxygenases. The same oxidants are produced during O<jats:sub>2</jats:sub> reduction during respiration in the mitochondria but are reduced by electron transfer i.e. reductases. Iron porphyrin mimics of the active site of Cytochrome P450 (Cyt P450) are created atop self-assembled monolayer covered electrode. The rate of electron transfer from the electrode to the iron porphyrin site is attenuated to derive monooxygenase reactivity from these constructs which generally show reductase activity and catalytic hydroxylation of inert C-H bonds to alcohol and epoxidation alkenes, using molecular O<jats:sub>2</jats:sub>, is demonstrated with turnover numbers > 10<jats:sup>4</jats:sup>. Mechanistic investigations suggest that a compound I analogue, formed during O<jats:sub>2</jats:sub> reduction, is the primary oxidant and the selectivity is determined by the shape of the distal environment of the catalyst. </jats:p>