Catalytic promiscuity of two novel cobalt(III) complexes derived from redox non-innocent Schiff base ligands: Unraveling the role of methyl groups in the ligand backbone on catalytic efficiency

Executing a Series of Zinc(II) Complexes of Homologous Schiff Base Ligands for a Comparative Analysis on Hydrolytic, Antioxidant, and Antibacterial Activities

“…Phosphatase is an assemblage of hydrolytic enzymes that catalyze the dephosphorylation reaction, that is, hydrolysis of phosphate monoesteric, diesteric, and triesteric P–O bonds − This is one of the essential biological reactions, as this is involved in cellular signaling, synthesis of proteins, replication of genetic material to energy, and so forth. , The uncatalyzed hydrolysis is extremely slow and the cleavage of P–O bonds is accelerated in the presence of bivalent metal ions. − Over the last few decades, many groups including our group have been involved in designing the bio-mimicking models to establish plausible mechanistic pathways of phosphatase activity. − Generally, dinuclear complexes are more efficient than their mononuclear counterparts because two metal centers may act mutually in substrate binding to catalyst, activation of the nucleophile, and cleavage of the bond. − The availability of a nucleophile (water or hydroxo) in the close vicinity of the metal center(s) is the predominant factor of phosphatase activity and attack of nucleophile on the phosphorus center is the rate-determining step of hydrolysis . The other factors that dictate the rate of hydrolysis are reaction conditions, Lewis acidity of metal centers, stereochemistry, presence of oxo-anions, the coordination domain of metal ions, and the presence of electronegative atoms in the ligand backbone. − In recent times, designing of bio-mimicking models with additional biological applications always draws special attention of the bio-inorganic chemists . The incorporation of metals to the ligand system enhanced the biological activity of the overall entity.…”