Tuning the Geometric and Electronic Structure of Synthetic High-Valent Heme Iron(IV)-Oxo Models in the Presence of a Lewis Acid and Various Axial Ligands.

ABSTRACT: High-valent ferryl species (e.g., (Por)Fe^IV═O, Cmpd-II) are observed or proposed key oxidizing intermediates in the catalytic cycles of heme-containing enzymes (P-450s, peroxidases, catalases, and cytochrome c oxidase) involved in biological respiration and oxidative metabolism. Herein, various axially ligated iron(IV)-oxo complexes were prepared to examine the influence of the identity of the base. These were generated by addition of various axial ligands (1,5-dicyclohexylimidazole (DCHIm), a tethered-imidazole system, and sodium derivatives of 3,5-dimethoxyphenolate and imidazolate). Characterization was carried out via UV-vis, electron paramagnetic resonance (EPR), ⁵⁷Fe Mössbauer, Fe X-ray absorption (XAS), and ^54/57Fe resonance Raman (rR) spectroscopies

SUBMITTER: Ehudin MA 

PROVIDER: S-EPMC6611672 | biostudies-literature | 2019 Apr

REPOSITORIES: biostudies-literature