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Two yellow air-stable mononuclear dioxomolybdenum(VI) complexes, MoO 2 Cl 2 L ( 1 ) and MoO 2 Br 2 L ( 2 ) [where L = N,N donor ligand 2-(3-methyl-5-phenyl pyrazol-1-yl) benzthiazole], have been synthesized from their parent oxomolybdenum(V) complexes in dichloromethane. The binding affinity and binding mode of the molybdenum complexes with bovine serum albumin (BSA) have been explored by absorption and fluorescence titrations and time resolved fluorescence measurements. The number of binding sites for the complexes is nearly equal to unity, indicating there is only one binding site per BSA molecule. Molecular docking studies are also carried out to elucidate the binding mechanism, indicating that the complexes could quench the intrinsic fluorescence of BSA in a static quenching manner. Fluorescence resonance energy transfer study reveals that energy transfer takes place from Tryptophan residue of BSA to the synthesized complexes. The anti-oxidative properties of the complexes are examined by ABTS radical scavenging activities and DPPH radical quenching. The complexes exhibit different activities due to the influence of halogen substitution to the metal ion. MoO 2 Br 2 L ( 2 ) exhibits better activities than MoO 2 Cl 2 L ( 1 ) according to their EC 50  values.

journal of coordination chemistry

Protein binding studies and antioxidant activities of two mononuclear dioxomolybdenum(VI) complexes with 2-(3-methyl-5-phenyl pyrazol-1-yl) benzthiazole