Successful clinical experience of using transition metal complexes in cancer therapy has encouragedscientists to synthesize new metal complexes with the aim of interacting with special targets such asproteins [1,2].In this regard, biological effects of [Pd(dach)(FIP)](NO3)2 compound  which contains anovel phen-imidazole ligand, FIP, was investigated on bovine liver Catalase (BLC) structure andfunction. Various spectroscopic methods such as UV–visible, fluorescence, and circular dichroism
(CD)were applied at different temperatures of 25 and 37 °C for kinetics and structural studies. As aconsequence, the enzymatic activity
slightly decreased with increasing palladium compound’sconcentration only to 0.03 mM and fortunately remained constant at near 70% after this concentration.Also, the fluorescence
quenching measurements revealed that despite slight changes in activity, catalaseexperiences notable alterations in three-dimensional environment around the chromophores of the enzymestructure with increasing palladium complex concentration.Moreover, Quenching data showed that BLChas one binding sites for Pd in 25˚C and two sites in 37˚C and hydrophobic interaction play a major rolein the binding process. Furthermore, CD spectroscopy data showed that Pd complex induces slightchanges in the secondary structure of BLC. Regarding the vital anticancer bioactivity of catalase, i.e.breast cancer, this might be a promising outcome for chemotherapists and medicinal chemists who areinvestigating on metal complexes with anticancer activity and no side effects to do in vivo studies on thisnovel-imidazole derivative of palladium that has a notable tendency to bind to a macromolecule in thelow concentrations.