Acetylacetone dioxygenase (Dkel) is a bacterial enzyme that catalyzes the dioxygen-dependent degradation of beta-dicarbonyl compounds. The Dkel 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 beta-diketonato complexes that faithfully mimic the enzyme-substrate intermediate of Dkel (Park, H.; Baus, J.S.; Lindeman, S.V.; Fiedler, A.T. Inorg. Chem. 2011, 50, 11978-11989). The 3His triad was modeled with three different facially coordinating N3 supporting ligands, and substituted beta-diketonates (acac(x)) with varying steric and electronic properties were employed. Here, we describe the reactivity of our Dkel models toward O-2 and its surrogate nitric oxide (NO), and report the synthesis of three new Fe(II) complexes featuring the anions of dialkyl malonates. Exposure of [Fe((Me2)Tp)(acac(x))] complexes (where (R2)Tp = hydrotris(pyrazol-1-yl)borate with R-groups at the 3- and 5-positions of the pyrazole rings) to O-2 at -70 degrees C in toluene results in irreversible formation of green chromophores (lambda(max) similar to 750 nm) that decay at temperatures above -60 degrees C. Spectroscopic and computational analyses suggest that these intermediates contain a diiron(III) unit bridged by a trans mu-1,2-peroxo ligand. The green chromophore is not observed with analogous complexes featuring (Ph2)Tp and (TIP)-T-Ph ligands (where (TIP)-T-Ph = tris(2-phenylimidazoly-4-yl)phosphine), since the steric bulk of the phenyl substituents prevents formation of dinuclear species. While these complexes are largely inert toward O-2, (Ph2)Tp-based complexes with dialkyl malonate anions exhibit dioxygenase activity and thus serve as functional Dkel models. The Fe/acac(x) complexes all react readily with NO to yield high-spin (S = 3/2) {FeNO}(7) adducts that were characterized with crystallographic, spectroscopic, and computational methods. Collectively, the results presented here enhance our understanding of the chemical factors involved in the oxidation of aliphatic substrates by nonheme iron dioxygenases.