Unprecedented HAT rate acceleration in water by a non-heme manganese oxo complex.

ABSTRACT: Nature employs water as the reaction medium for enzymatic redox transformations, taking advantage of its unique physicochemical properties to precisely regulate reaction kinetics, selectivity, and proton-coupled electron transfer. In a biomimetic endeavour, using a newly developed non-heme (Et₄N)[Mn^V(O)(Ph,Me-bTAML)] complex, we report a water-induced, enzyme-like rate acceleration in hydrogen atom transfer (HAT) reactivity with various substrates possessing BDEs of 67-78 kcal mol^-1. In acetonitrile, the reactivity is sluggish, but switching to water - particularly beyond 85% content - results in a dramatic rate enhancement, peaking in pure water with up to a 20 000-fold increase. This effect occurs without any structural changes or addition of external add

SUBMITTER: De P 

PROVIDER: S-EPMC12766740 | biostudies-literature | 2026 Feb

REPOSITORIES: biostudies-literature