Abstract
The first iron complex capable of olefin cis-dihydroxylation in combination with H(2)O(2) provides a functional model for Rieske dioxygenases. Mechanistic studies on the model reaction suggest the participation of an Fe(III)(eta(2)-OOH) intermediate, with the oxygen atoms coming exclusively from H(2)O(2) (see reaction scheme; L denotes a tris(6-methyl-2-pyridylmethyl)amine ligand, Solv=solvent). The similarities between the model and the enzymes strengthen the proposal that an Fe(III)-peroxo intermediate is involved in the enzymatic reactions.
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