Abstract
Oxovanadium(IV) complexes with aroylhydrazine ligands have been synthesized. Structural elucidation of synthesized complexes is carried out with the help of various physical, chemical and spectral analysis. Dimeric nature of synthesized complexes further characterized by effective magnetic moments, spectral, conductance, CHN and metal analysis. In the current study we examined 1c to 10c vanadium (IV)-aroylhydrazine complexes for their mechanism of inhibition with the nickel containing active sites of Canavalia ensiformis (Jack bean) and Bacillus pasteurii ureases. Inhibition of both urease enzymes by compounds 1c-10c are depends on concentration. Lineweaver-Burk as well as Dixon plots and their secondary replots indicated that the mechanisms of inhibition exhibited by vanadium complexes 1c-10c are very diverse. The Ki values ranging from 15.1-79.3 mu M for Canavalia ensiformis urease while for Bacillus pasteurii urease 25.2-123.7 mu M. The model presented here is evidenced by biochemical enzyme kinetics data. Efforts are made to obtain significant approach into the pharmacophore needs of urease. The high affinity of these vanadium complexes along with their safe profile against plants could make them promising lead candidates and provides fertile ground for future research.