Reactivities of mononuclear non-heme iron intermediates including evidence that iron(III) hydroperoxo species is a sluggish oxidant

There is an intriguing, current controversy on the involvement of iron(III)-hydroperoxo species as a "second electrophilic oxidant" in oxygenation reactions by heme and non-heme iron enzymes and their model compounds. In the present work, we have performed reactivity studies of the iron-hydroperoxo species in nucleophilic and electrophilic reactions, with in situ-generated mononuclear non-heme iron(III)-hydroperoxo complexes that have been well characterized with various spectroscopic techniques. The intermediates did not show any reactivities in the nucleophilic (e.g., aldehyde deformylation) and electrophilic (e.g., oxidation of sulfide and olefin) reactions. These results demonstrate that non-heme iron(III)-hydroperoxo species are sluggish oxidants and that the oxidizing power of the intermediates cannot compete with that of high-valent iron(IV)-oxo complexes. We have also reported reactivities of mononuclear non-heme iron(III)-peroxo and iron(IV)-oxo complexes in the aldehyde deformylation and the oxidation of sulfides, respectively.