Journal
INORGANIC CHEMISTRY
Volume 44, Issue 1, Pages 85-99Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ic0485312
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- NIGMS NIH HHS [GM-38767] Funding Source: Medline
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A series of complexes with [Fe-2(II)(mu-OH)(2)]) cores has been synthesized with N3 and N4 ligands and structurally characterized to serve as models for nonheme diiron(II) sites in enzymes that bind and activate O-2. These complexes react with O-2 in solution via bimolecular rate-limiting steps that differ in rate by 10(3)-fold, depending on ligand denticity and steric hindrance near the diiron center. Low-temperature trapping of a (mu-oxo)(mu-1,2-peroxo)diiron(III) intermediate after O-2 binding requires sufficient steric hindrance around the diiron center and the loss of a proton (presumably that of a hydroxo bridge or a yet unobserved hydroperoxo intermediate). The relative stability of these and other (mu-1,2-peroxo)diiron(III) intermediates suggests that these species may not be on the direct pathway for dioxygen activation.
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