Zinc is an essential trace element vital for many physiological functions. In the present study, DNA binding and cleavage activities of a novel Zn-flavonol complex was investigated. The interaction of the complex with CT-DNA has been explored by absorption, emission, viscosity and circular dichoric measurements. The complex exhibited hypochromicity in absorption and an increase in specific viscosity, which revealed that the complex bound to CTDNA through an intercalation mode. The calculated intrinsic binding constant (Kb) was found to be 6.2 x 104 M-1. The data revealed that the complex facilitates the cleavage of super coiled pBR322 DNA (Form I) to the open circular form (Form II) and linear form (Form III) via a hydrolytic pathway. Further, the synthesized complexes altered the intrinsic fluorescence of bovine serum albumin (BSA) through a static quenching with the binding constants (Ksv) of 1.6 x 105 M-1 with a number of binding sites of 0.98.