•A novel acetylhydroxamate coordinated oxovanadium(V) complex was prepared.•The complex has been characterized by single crystal X-ray diffraction.•Thermal stability was studied.•The complex shows strong urease inhibitory activity.The first example of a novel acetylhydroxamate-coordinated oxovanadium(V) complex with hydrazone ligand has been prepared and structurally characterized. The urease inhibitory activity of the complex was assayed, and the molecular docking study was performed. The complex has strong urease inhibitory activity. The introduction of acetylhydroxamate ligand as functional urease inhibitory group may increase the activity of the complex.The first example of a novel acetylhydroxamate coordinated oxovanadium(V) complex with hydrazone ligand was obtained. The complex shows strong urease inhibitory activity with IC50 value of 8.3 ± 1.6 μM.

A new oxovanadium(V) complex [VOL(BZH)] was prepared by the reaction of [VO(Acac)2] (Acac = acetylacetonate) with N′-(3,5-dibromo-2-hydroxybenzylidene)isonicotinohydrazide (H2L) and benzohydroxamic acid (HBZH) in methanol. Crystal and molecular structure of the complex was determined by elemental analysis, infrared spectra and single crystal X-ray diffraction. The complex crystallizes in the monoclinic space group P21/c, with unit cell dimensions a = 11.424(1), b = 12.012(1), c = 19.565(2) Å, β = 93.487(3)°, V = 2679.8(4) Å3, Z = 4, GOOF = 1.152, R1 = 0.0593, and wR2 = 0.1942. The V atom is in octahedral coordination. Thermal stability and the inhibition of urease of the complex were studied.

A new acetohydroxamate-coordinated oxovanadium(V) complex, [VOL(AE)] (1), and a new benzohydroxamate-coordinated oxovanadium(V) complex, [VOL(BE)] (2), where L is the dianionic form of N′-(2-hydroxy-5-methylbenzylidene)-2-methoxybenzohydrazide, have been synthesized and characterized by physicochemical methods and single-crystal X-ray diffraction. The V atom in each complex adopts octahedral coordination. Thermal stabilities and urease inhibitory activities of the complexes were studied. The percent inhibition of complexes 1 and 2 at the concentration of 100 μmol L−1 on Helicobacter pylori urease is 81.2 and 46.7 %, respectively. Complex 1 has an IC50 value of 27.0 μmol L−1. A molecular docking study of the complexes with the H. pylori urease was performed.