To date, artificial dioxygen adducts of heme 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.

Phenols and quinols participate in both proton transfer and electron transfer processes in nature either in distinct elementary steps or in a concerted fashion. Recent investigations using synthetic heme/Cu models and iron porphyrins have indicated that phenols/quinols can react with both ferric superoxide and ferric peroxide intermediates formed during O 2 reduction through a proton coupled electron transfer (PCET) process as well as via hydrogen atom transfer (HAT). Oxygen reduction by iron porphyrins bearing covalently attached pendant phenol and quinol groups is investigated. The data show that both of these can electrochemically reduce O 2 selectively by 4e − /4H + to H 2 O with very similar rates. However, the mechanism of the reaction, investigated both using heterogeneous electrochemistry and by trapping intermediates in organic solutions, can be either PCET or HAT and is governed by the thermodynamics of these intermediates involved. The results suggest that, while the reduction of the Fe III −O 2 − species to Fe III −OOH proceeds via PCET when a pendant phenol is present, it follows a HAT pathway with a pendant quinol. In the absence of the hydroxyl group the O 2 reduction proceeds via an electron transfer followed by proton transfer to the Fe III −O 2 − species. The hydrogen bonding from the pendant phenol group to Fe III −O 2 − and Fe III −OOH species provides a unique advantage to the PCET process by lowering the inner-sphere reorganization energy by limiting the elongation of the O−O bond upon reduction.

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Activation of inert C-H bonds such as those of methane are extremely challenging for chemists but in nature, the soluble methane monooxygenase (sMMO) enzyme readily oxidizes methane to methanol by using a diiron(IV) species. This has prompted chemists to look for similar model systems. Recently, a (μ-oxo)bis(μ-carboxamido)diiron(IV) ([Fe O(L) ] L=N,N-bis-(3',5'-dimethyl-4'-methoxypyridyl-2'-methyl)-N'-acetyl-1,2-diaminoethane) complex has been generated by bulk electrolysis and this species activates inert C-H bonds almost 1000 times faster than mononuclear Fe =O species and at the same time selectively activates O-H bonds of alcohols. The very high reactivity and selectivity of this species is puzzling and herein we use extensive DFT calculations to shed light on this aspect. We have studied the electronic and spectral features of diiron {Fe -μ(O)-Fe } (complex I), {Fe -μ(O)-Fe } (II), and {Fe -μ(O)-Fe } (III) complexes. Strong antiferromagnetic coupling between the Fe centers leads to spin-coupled S=0, S=3/2, and S=0 ground state for species I-III respectively. The mechanistic study of the C-H and O-H bond activation reveals a multistate reactivity scenario where C-H bond activation is found to occur through the S=4 spin-coupled state corresponding to the high-spin state of individual Fe centers. The O-H bond activation on the other hand, occurs through the S=2 spin-coupled state corresponding to an intermediate state of individual Fe centers. Molecular orbital analysis reveals σ-π/π-π channels for the reactivity. The nature of the magnetic exchange interaction is found to be switched during the course of the reaction and this offers lower energy pathways. Significant electronic cooperativity between two metal centers during the course of the reaction has been witnessed and this uncovers the reason behind the efficiency and selectivity observed. The catalyst is found to prudently choose the desired spin states based on the nature of the substrate to effect the catalytic transformations. These findings suggest that the presence of such factors play a role in the reactivity of dinuclear metalloenzymes such as sMMO.