Dramatic rate-enhancement of oxygen atom transfer by an iron(iv)-oxo species by equatorial ligand field perturbations.

摘要: Nonheme iron dioxygenases are efficient enzymes with relevance for human health that regio- and stereospecifically transfer an oxygen atom to substrates. How they perform this task such selectivity remains unknown, but may have do substrate binding, positioning oxidant approach. To understand approach on a catalytic reaction centre, we investigated the structure reactivity of biomimetic ligand features affect interactions between substrate. Thus, report here synthesis characterization iron(iv)-oxo complex pentadentate nonheme ligand, where structurally induced perturbations in equatorial field spectroscopy complex. We tested activity respect hydrogen abstraction from This shows improved rates toward heteroatom oxidation nonsubstituted by ∼104 fold. The origin enhanced is explained series density functional theory studies show electron affinity through perturbations.