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

ABSTRACT: 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.; 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 β-diketonates (acac(X)) with varying steric and electronic properties were em

SUBMITTER: Park H 

PROVIDER: S-EPMC3965333 | biostudies-literature | 2012 Oct

REPOSITORIES: biostudies-literature