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Research Article

Enzyme inhibition, radical scavenging, and spectroscopic studies of vanadium(IV)–hydrazide complexes

, , , , , & show all
Pages 1336-1343 | Received 19 Jul 2008, Accepted 10 Mar 2009, Published online: 16 Nov 2009
 

Abstract

Spectroscopic, enzyme-inhibition, and free-radical scavenging properties of a series of hydrazide ligands and their vanadium(IV) complexes have been investigated. Analytical and spectral data indicate the presence of a dimeric unit with two oxovanadium(IV) ions (VO2+) coordinated with two hydrazide ligands along with two water molecules. All complexes are stable in the solid state, but exhibit varying degrees of stability in solution. Binding of the coordinating solvent such as DMSO is indicated at the 6th position of vanadium in the dimeric unit followed by conversion to a monomeric intermediate species, [VOL(DMSO)3]1+ (L = hydrazide ligand). The free hydrazide ligands are inactive against snake venom phosphodiesterase I (SVPD), whereas oxovanadium(IV) complexes of these ligands show varying degrees of inhibition and are found to be non-competitive inhibitors. The superoxide and nitric oxide radical scavenging properties have been determined. Hydrazide ligands are inactive against these free radicals, whereas their V(IV) complexes show varying degrees of inhibition. Structure–activity relationship studies indicate that the electronic and/or steric factors that change the geometry of the complexes play an important role in their inhibitory potential against SVPD and free radicals.

Acknowledgments

The authors are thankful to the Higher Education Commission (HEC), Pakistan, for financial support under “National Research Grants Program for Universities”, Grant No. 20-224/2nd Phase/R&D/03/442, and the Ministry of Labour, Manpower and Overseas Pakistanis National Talent Pool for the visit of M.M.T.

Declaration of interest: The authors report no conflicts of interest.

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