Abstract
A novel Schiff base namely, (Z)-4-((3-cyano-4,6-dimethylpyridin-2-yl)amino)-N'-(2-oxoindolin-3-ylidene)benzohydrazide (H(2)BISH) (C1) and its corresponding metal acetate chelates; [Co(2)(HBISH)(CH(3)COO)(3)(H(2)O)(2)]·H(2)O (C2), [Ni(HBISH)(CH(3)COO)]·2.5H(2)O (C3) and [Cu(HBISH)(CH(3)COO)(H(2)O)] (C4) were prepared and characterized using elemental and spectroscopic (IR, UV-vis., nuclear magnetic resonance ((1)H&(13)C), electron paramagnetic resonance (ESR), mass and XRD measurements. IR spectral data revealed that H(2)BISH acts as monobasic in all metal complexes. The (1)HNMR chemical shifts of the ligand protons are relatively well reproduced at the HF/6-31G(d) level of theory. Ni(2+) complex (C1) adopted a tetrahedral structure while Co(2+) (C2) and Cu(2+) complexes assigned an octahedral one. The structure of C2 was further investigated by XRD technique orthorhombic C(30) Co(3) N(22)O(5) geometry with lattice constants a = 6.5688 Å, b = 31.7110 Å and c = 18.1864 Å and Cm c m space group. Kinetic parameters of thermal degradation of studied compounds were evaluated by Coats-Redfern and Horowitz-Metzger equations. Density function theory was utilized to draw the structures and evaluate the correlated parameters. All title compounds have small negative E(g) of order: C2 < C3 < C4 < C1 (H(2)BISH) revealing the ease of CT in turn the higher polarizability, increased reactivity and softness as well as the values lie in the range of semiconductor suggesting the possibility of utilization of present compounds in solar cells. The compounds were tested for antioxidant power (DPPH free radical scavenger assay) and bacterial inhibition against Bacillus cereus as Gram + ve and Escherichia coli as Gram - ve bacteria. A molecular docking mechanism between the ligand and its M(2+) chelating was evaluated against bacterial proteins and Breast cancer cells sites receptors to explain how these compounds attach the protein's active sites. The findings showed promising binding.