Set of Fe(II)-3-Hydroxyflavonolate Enzyme–Substrate Model Complexes of Atypically Coordinated Mononuclear Non-Heme Fe(II)-Dependent Quercetin 2,4-Dioxygenase

[Image: see text] With the aim of revealing the catalytic role of atypically coordinated (3His-1Glu) active site mononuclear non-heme Fe(II)-dependent quercetin 2,4-dioxygenase (Fe-2,4-QD) and the electronic effects of the model ligands on the reactivity toward dioxygen, a set of p/m-R-substituted carboxylate-containing ligand-supported Fe(II)-3-hydroxyflavonolate complexes, [Fe(II)L(R)(fla)] (L(R)H: 2-{[bis(pyridin-2-ylmethyl)amino]methyl}-p/m-R-benzoic acid; R: p-OMe (1), p-Me (2), m-Br (4), and m-NO(2) (5); fla: 3-hydroxyflavonolate), were synthesized and characterized as structural and functional models for the ES (enzyme–substrate) complexes of Fe-2,4-QD. [Fe(II)L(R)(fla)] show relatively high enzyme-type reactivity (dioxygenative ring opening of the coordinated substrate fla, single-turnover reaction) at low temperatures (30–65 °C). The reaction shows a linear Hammett plot (ρ = −1.21), and electron donating groups enhance the reaction rates. The notable difference on the reactivity can be rationalized from the electronic nature of the substituent in the ligands, which could tune the reactivity via tuning Lewis acidity of the Fe(II) ion, electron density, and the redox potential of fla. The properties and the reactivity show approximately linear correlations between λ(max) or E(1/2) of fla and the reaction rate constant k. This work sheds light not only on understanding of electronic effects of the ligands and the property–reactivity relationship but also on the role of the catalytic reaction by Fe-2,4-QD.