Oxygen Delivery as a Limiting Factor in Modelling Dicopper(II) Oxidase Reactivity

Deprotonation of ligand-appended alkoxyl groups in mononuclear copper(II) complexes of N,O ligands L₁ and L₂ , gave dinuclear complexes sharing symmetrical Cu₂ O₂ cores. Molecular structures of these mono- and binuclear complexes have been characterized by XRD, and their electronic structures by UV/Vis, ¹ H NMR, EPR and DFT; moreover, catalytic performance as models of catechol oxidase was studied. The binuclear complexes with anti-ferromagnetically coupled copper(II) centers are moderately active in quinone formation from 3,5-di-tert-butyl-catechol under the established conditions of oxygen saturation, but are strongly activated when additional dioxygen is administered during catalytic turnover. This unforeseen and unprecedented effect is attributed to increased maximum reaction rates v_max , whereas the substrate affinity K_M remains unaffected. Oxygen administration is capable of (partially) removing limitations to turnover caused by product inhibition. Because product inhibition is generally accepted to be a major limitation of catechol oxidase models, we think that our observations will be applicable more widely.