1 research outputs found
Reactivity of an Fe<sup>IV</sup>-Oxo Complex with Protons and Oxidants
High-valent Fe-OH
species are often invoked as key intermediates
but have only been observed in Compound II of cytochrome P450s. To
further address the properties of non-heme Fe<sup>IV</sup>-OH complexes,
we demonstrate the reversible protonation of a synthetic Fe<sup>IV</sup>-oxo species containing a tris-urea tripodal ligand. The same protonated
Fe<sup>IV</sup>-oxo species can be prepared via oxidation, suggesting
that a putative Fe<sup>V</sup>-oxo species was initially generated.
Computational, Mössbauer, XAS, and NRVS studies indicate that
protonation of the Fe<sup>IV</sup>-oxo complex most likely occurs
on the tripodal ligand, which undergoes a structural change that results
in the formation of a new intramolecular H-bond with the oxido ligand
that aids in stabilizing the protonated adduct. We suggest that similar
protonated high-valent Fe-oxo species may occur in the active sites
of proteins. This finding further argues for caution when assigning
unverified high-valent Fe-OH species to mechanisms