Characterized cis-Fe^V(O)(OH) intermediate mimics enzymatic oxidations in the gas phase.

ABSTRACT: Fe^V(O)(OH) species have long been proposed to play a key role in a wide range of biomimetic and enzymatic oxidations, including as intermediates in arene dihydroxylation catalyzed by Rieske oxygenases. However, the inability to accumulate these intermediates in solution has thus far prevented their spectroscopic and chemical characterization. Thus, we use gas-phase ion spectroscopy and reactivity analysis to characterize the highly reactive [Fe^V(O)(OH)(^5tips3tpa)]²⁺ (3²⁺) complex. The results show that 3²⁺ hydroxylates C-H bonds via a rebound mechanism involving two different ligands at the Fe center and dihydroxylates olefins and arenes. Hence, this study provides a direct evidence of Fe^V(O)(OH) species in non-he

SUBMITTER: Borrell M 

PROVIDER: S-EPMC6385299 | biostudies-literature | 2019 Feb

REPOSITORIES: biostudies-literature