Abstract
The iron oxo unit, [Fe=O]n+ is a critical intermediate in biological oxidation reactions. While its higher oxidation states are well studied, relatively little is known about the least-oxidized form [FeIII=O]+. Here, the thermally stable complex PhB(AdIm)3Fe=O has been structurally, spectroscopically, and computationally characterized as a bona fide iron(III) oxo. An unusually short Fe–O bond length is consistent with iron–oxygen multiple bond character and is supported by electronic structure calculations. The complex is thermally stable yet is able to perform hydrocarbon oxidations, facilitating both C–O bond formation and dehydrogenation reactions.
Highlights
The iron oxo unit, [Fe O]n+ is a critical intermediate in biological oxidation reactions
Iron(IV) oxo species, [FeIV=O]2+, are key intermediates in biological C−H oxidation reactions catalyzed by nonheme iron-containing oxygenases.[1,2]
Studies of model compounds reveal that hydrocarbon oxidation is initiated by hydrogen atom transfer (HAT) to the oxo ligand, generating the corresponding iron(III) hydroxide, [FeIII−OH]2+.3−7 While hydrogen atom transfer in these reactions usually occurs by a concerted mechanism, for certain substrates a stepwise pathway has been proposed.[8,9]
Summary
The iron oxo unit, [Fe O]n+ is a critical intermediate in biological oxidation reactions. A handful of iron(III) oxo complexes have been structurally characterized, but it is notable that these all feature secondcoordination sphere hydrogen-bond donors that stabilize and shield the oxo ligand,[12−14] thereby masking its reactivity.
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