O–H bond oxidation by a monomeric MnIII–OMe complex

Abstract

Manganese-containing, mid-valent oxidants (Mn^III–OR) that mediate proton-coupled electron-transfer (PCET) reactions are central to a variety of crucial enzymatic processes. The Mn-dependent enzyme lipoxygenase is such an example, where a Mn^III–OH unit activates fatty acid substrates for peroxidation by an initial PCET. This present work describes the quantitative generation of the Mn^III–OMe complex, [Mn^III(OMe)(dpaq)]⁺ (dpaq = 2-[bis(pyridin-2-ylmethyl)]amino-N-quinolin-8-yl-acetamidate) via dioxygen activation by [Mn^II(dpaq)]⁺ in methanol at 25 °C. The X-ray diffraction structure of [Mn^III(OMe)(dpaq)]⁺ exhibits a Mn–OMe group, with a Mn–O distance of 1.825(4) Å, that is trans to the amide functionality of the dpaq ligand. The [Mn^III(OMe)(dpaq)]⁺ complex is quite stable in solution, with a half-life of 26 days in MeCN at 25 °C. [Mn^III(OMe)(dpaq)]⁺ can activate phenolic O–H bonds with bond dissociation free energies (BDFEs) of less than 79 kcal mol⁻¹ and reacts with the weak O–H bond of TEMPOH (TEMPOH = 2,2′-6,6′-tetramethylpiperidine-1-ol) with a hydrogen/deuterium kinetic isotope effect (H/D KIE) of 1.8 in MeCN at 25 °C. This isotope effect, together with other experimental evidence, is suggestive of a concerted proton-electron transfer (CPET) mechanism for O–H bond oxidation by [Mn^III(OMe)(dpaq)]⁺. A kinetic and thermodynamic comparison of the O–H bond oxidation reactivity of [Mn^III(OMe)(dpaq)]⁺ to other M^III–OR oxidants is presented as an aid to gain more insight into the PCET reactivity of mid-valent oxidants. In contrast to high-valent counterparts, the limited examples of M^III–OR oxidants exhibit smaller H/D KIEs and show weaker dependence of their oxidation rates on the driving force of the PCET reaction with O–H bonds.