Dioxygen reactivity of biomimetic Fe(II) complexes with noninnocent catecholate, o-aminophenolate, and o-phenylenediamine ligands.

This study describes the O2 reactivity of a series of high-spin mononuclear Fe(II) complexes each containing the facially coordinating tris(4,5-diphenyl-1-methylimidazol-2-yl)phosphine ((Ph2)TIP) ligand and one of the following bidentate, redox-active ligands: 4-tert-butylcatecholate ((tBu)CatH(-)), 4,6-di-tert-butyl-2-aminophenolate ((tBu2)APH(-)), or 4-tert-butyl-1,2-phenylenediamine ((tBu)PDA). The preparation and X-ray structural characterization of [Fe(2+)((Ph2)TIP)((tBu)CatH)]OTf, [3]OTf and [Fe(2+)((Ph2)TIP)((tBu)PDA)](OTf)2, [4](OTf)2 are described here, whereas [Fe(2+)((Ph2)TIP)((tBu2)APH)]OTf, [2]OTf was reported in our previous paper [Bittner et al., Chem.

Synthetic, spectroscopic, and DFT studies of iron complexes with iminobenzo(semi)quinone ligands: implications for o-aminophenol dioxygenases.

The oxidative C-C bond cleavage of o-aminophenols by nonheme Fe dioxygenases is a critical step in both human metabolism (the kynurenine pathway) and the microbial degradation of nitroaromatic pollutants. The catalytic cycle of o-aminophenol dioxygenases (APDOs) has been proposed to involve formation of an Fe(II)/O2/iminobenzosemiquinone complex, although the presence of a substrate radical has been called into question by studies of related ring-cleaving dioxygenases. Recently, we reported the first synthesis of an iron(II) complex coordinated to an iminobenzosemiquinone (ISQ) ligand, namely, [Fe((Ph2)Tp)((tBu)ISQ)] (2a; where (Ph2)Tp=hydrotris(3,5-diphenylpyrazol-1-yl)borate and (tBu)ISQ is the radical anion derived from 2-amino-4,6-di-tert-butylphenol).

Fe(II) complexes that mimic the active site structure of acetylacetone dioxygenase: O2 and NO reactivity.

Acetylacetone dioxygenase (Dke1) is a bacterial enzyme that catalyzes the dioxygen-dependent degradation of β-dicarbonyl compounds. The Dke1 active site contains a nonheme monoiron(II) center facially ligated by three histidine residues (the 3His triad); coordination of the substrate in a bidentate manner provides a five-coordinate site for O(2) binding. Recently, we published the synthesis and characterization of a series of ferrous β-diketonato complexes that faithfully mimic the enzyme-substrate intermediate of Dke1 (Park, H.

A synthetic model of the putative Fe(II)-iminobenzosemiquinonate intermediate in the catalytic cycle of o-aminophenol dioxygenases.

The oxidative ring cleavage of aromatic substrates by nonheme Fe dioxygenases is thought to involve formation of a ferrous-(substrate radical) intermediate. Here we describe the synthesis of the trigonal-bipyramdial complex Fe((Ph2)Tp)(ISQ(tBu)) (2), the first synthetic example of an iron(II) center bound to an iminobenzosemiquinonate (ISQ) radical. The unique electronic structure of this S = 3/2 complex and its one-electron oxidized derivative ([3](+)) have been established on the basis of crystallographic, spectroscopic, and computational analyses.