A Pseudotetrahedral Terminal Oxoiron(IV) Complex: Mechanistic Promiscuity in C−H Bond Oxidation Reactions. (15th February 2021)

• Record Type: Journal Article
• Authors: Warm, Katrin; Paskin, Alice; Kuhlmann, Uwe; Bill, Eckhard; Swart, Marcel; Haumann, Michael; Dau, Holger; Hildebrandt, Peter; Ray, Kallol
• Is Part Of: Angewandte Chemie. Volume 133:Number 12(2021)
• Page Start: 6826
• Page End: 6830
• Publication Date: 2021-02-15
• Subjects: bioinorganic chemistry -- enzyme models -- high-valent iron -- hydrogen atom abstraction -- electron transfer; Chemistry -- Periodicals; 540
• DOI: 10.1002/ange.202015896
• Languages: English
• ISSNs: 0044-8249

Abstract

Abstract: S= 2 oxoiron(IV) species act as reactive intermediates in the catalytic cycle of nonheme iron oxygenases. The few available synthetic S =2 Fe IV =O complexes known to date are often limited to trigonal bipyramidal and very rarely to octahedral geometries. Herein we describe the generation and characterization of an S =2 pseudotetrahedral Fe IV =O complex 2 supported by the sterically demanding 1, 4, 7‐tri‐ tert ‐butyl‐1, 4, 7‐triazacyclononane ligand. Complex 2 is a very potent oxidant in hydrogen atom abstraction (HAA) reactions with large non‐classical deuterium kinetic isotope effects, suggesting hydrogen tunneling contributions. For sterically encumbered substrates, direct HAA is impeded and an alternative oxidative asynchronous proton‐coupled electron transfer mechanism prevails, which is unique within the nonheme oxoiron community. The high reactivity and the similar spectroscopic parameters make 2 one of the best electronic and functional models for a biological oxoiron(IV) intermediate of taurine dioxygenase (TauD‐ J ). Abstract : A highly reactive S =2 pseudotetrahedral oxoiron(IV) complex 2 supported by a sterically demanding 1, 4, 7‐tri‐ tert ‐butyl‐1, 4, 7‐triazacyclononane ligand has been synthesized and spectroscopically characterized as one of the best electronic and functional models for a biological oxoiron(IV) intermediate of taurine dioxygenase (TauD‐ J ).