期刊
PHYSICAL CHEMISTRY CHEMICAL PHYSICS
卷 20, 期 45, 页码 28786-28795出版社
ROYAL SOC CHEMISTRY
DOI: 10.1039/c8cp05372c
关键词
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资金
- University of Tennessee
- National Science Foundation [CHE-1800237]
- Auburn University
High-valent Fe(iv)-oxo species have been found to be key oxidizing intermediates in the mechanisms of mononuclear iron heme and non-heme enzymes that can functionalize strong C-H bonds. Biomimetic Fe(iv)-oxo molecular complexes have been successfully synthesized and characterized, but their catalytic reactivity is typically lower than that of the enzymatic analogues. The C-H activation step proceeds through two competitive mechanisms, named sigma- and -channels. We have performed high-level wave function theory calculations on bare FeO2+ and a series of non-heme Fe(iv)-oxo model complexes in order to elucidate the electronic properties and the ligand field effects on those channels. Our results suggest that a coordination environment formed by a weak field gives access to both competitive channels, yielding more reactive Fe(iv)-oxo sites. In contrast, a strong ligand environment stabilizes only the sigma-channel. Our concluding remarks will aid the derivation of new structure-reactivity descriptors that can contribute to the development of the next generation of functional catalysts.
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