Nonheme oxo-iron(IV) intermediates form an oxyl radical upon approaching the C-H bond activation transition state.

ABSTRACT: Oxo-iron(IV) species are implicated as key intermediates in the catalytic cycles of heme and nonheme oxygen activating iron enzymes that selectively functionalize aliphatic C-H bonds. Ferryl complexes can exist in either quintet or triplet ground states. Density functional theory calculations predict that the quintet oxo-iron(IV) species is more reactive toward C-H bond activation than its corresponding triplet partner, however; the available experimental data on model complexes suggests that both spin multiplicities display comparable reactivities. To clarify this ambiguity, a detailed electronic structure analysis of alkane hydroxylation by an oxo-iron(IV) species on different spin-state potential energy surfaces is performed. According to our results, the lengthening of the Fe-oxo bond

SUBMITTER: Ye S 

PROVIDER: S-EPMC3029731 | biostudies-literature | 2011 Jan

REPOSITORIES: biostudies-literature