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Based on copper(II)-catalyzed reaction, the simple mixing of 1,2-cyclohexanedione-bis(p-chlorobenzohydrazone) (LCl) and copper(II) nitrate trihydrate in acetonitrile under ambient conditions produced a new mononuclear copper(II)-triazole ester complex as potent inhibitor for bacterial strains and urease enzyme. The prepared organic ligand and copper(II)-triazole ester complex can sufficiently reduce the activity of enzymes through some stable interactions with the functional residues in the active pockets. They can be considered as promising drug candidates for further structural optimizations and drug designing studies.
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The reaction of copper(II) nitrate trihydrate with N,Nʹ-cyclohexane-1,2-diylidene-bis(4-chlorobenzoylhydrazide) (LCl) in acetonitrile produced a mononuclear Cu(II) complex [CuII(TECl)2(NO3)2] (TECl: triazole-ester) (1). Triazole-ester is an intermediate compound formed during the oxidation of LCl by copper ion based on Cu(II) catalyzed click reaction. The organic ligand (LCl) and its complex (1) are characterized with different techniques. According to single crystal X-ray crystallography, complex 1 has been verified to possess a distorted square planar geometry and functions as a four-coordinate mononuclear copper(II) complex. Furthermore, the Cu(II) ion coordinates to the 1-N atoms of two monodentate (TECl) molecules, along with the N atoms of two monodentate nitrate ions. The optimization of geometry and other functional analyses was executed using density functional theory (DFT). Additionally, molecular electrostatic potential (MEP) and Hirshfeld surface analyses were conducted to scrutinize the reactive regions within the crystals. Employing molecular modeling software, the most suitable conformational bond between the prepared compounds (LCl and 1) and the urease enzyme is investigated to calculate the structure–activity relationship and binding energies. Moreover, comprehensive studies were performed on in vitro enzyme inhibition, pharmacokinetics, enzyme kinetic mechanism, and antimicrobial activity. These investigations revealed that the synthesized compounds exhibit a pronounced affinity for binding to the urease enzyme. Furthermore, the compounds demonstrate promising inhibitory potential against select bacterial strains and the urease enzyme, as evidenced by their MIC and IC50 values.