Generally, cobalt–N2O2 complexes show selectivity for hydrogen peroxide during electrochemical dioxygen (O2) reduction. We recently reported a Co­(III)–N2O2 complex with a 2,2′-bipyridine-based ligand backbone which showed alternative selectivity: H2O was observed as the primary reduction product from O2 (71 ± 5%) with decamethylferrocene as a chemical reductant and acetic acid as a proton donor in methanol solution. We hypothesized that the key selectivity difference in this case arises in part from increased favorability of protonation at the distal O position of the key intermediate Co­(III)–hydroperoxide species. To interrogate this hypothesis, we have prepared a new Co­(III) compound that contains pendent −OMe groups poised to direct protonation toward the proximal O atom of this hydroperoxo intermediate. Mechanistic studies in acetonitrile (MeCN) solution reveal two regimes are possible in the catalytic response, dependent on added acid strength and the presence of the pendent proton donor relay. In the presence of stronger acids, the activity of the complex containing pendent relays becomes O2 dependent, implying a shift to Co­(III)–superoxide protonation as the rate-determining step. Interestingly, the inclusion of the relay results in primarily H2O2 production in MeCN, despite minimal difference between the standard reduction potentials of the three complexes tested. EPR spectroscopic studies indicate the formation of Co­(III)–superoxide species in the presence of exogenous base, with greater O2 reactivity observed in the presence of the pendent −OMe groups.

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Traditionally, the ferritin-like superfamily of proteins was thought to exclusively use a diiron active site in catalyzing a diverse array of oxygen-dependent reactions. In recent years, novel redox-active cofactors featuring heterobimetallic Mn/Fe active sites have been discovered in both the radical-generating R2 subunit of class Ic (R2c) ribonucleotide reductases (RNRs) and the related R2like ligand-binding oxidases (R2lox). However, the protein-specific factors that differentiate the radical reactivity of R2c from the C−H activation reactions of R2lox remain unknown. In this work, multifrequency pulsed electron paramagnetic resonance (EPR) spectroscopy and ligand hyperfine techniques in conjunction with broken-symmetry density functional theory calculations are used to characterize the molecular and electronic structures of two EPR-active intermediates trapped during aerobic assembly of the R2lox Mn/Fe cofactor. A Mn III (μ-O)(μ-OH)Fe III species is identified as the first EPR-active species and represents a common state between the two classes of redox-active Mn/Fe proteins. The species downstream from the Mn III (μ-O)(μ-OH)Fe III state exhibits unique EPR properties, including unprecedented spectral breadth and isotope-dependent g-tensors, which are attributed to a weakly coupled, hydrogen-bonded Mn III (μ-OH)Fe III species. This final intermediate precedes formation of the Mn III /Fe III resting state and is suggested to be relevant to understanding the endogenous reactivity of R2lox.