Synthesis, urease inhibitory activities, and molecular docking studies of two Cu(II) complexes

Abstract

Two mononuclear copper(II) complexes, [Cu(C4H3N2O2)2 · 4H2O] (1) and [Cu(C12H11N2O2Cl2)2] (2), were synthesized and structurally characterized by single-crystal X-ray analysis. The copper(II) adopts a square-planar environment in 1, while the geometry in 2 can be described as distorted square-pyramidal. Complexes 1 and 2 were evaluated for their inhibitory activities against jack bean urease in vitro and both were found to have strong inhibitory activities comparable to that of acetohydroxamic acid. A docking simulation was performed to position 2 into the jack bean urease active site to determine the probable binding conformation.