Facile synthesis of novel NNO-tethered copper(<scp>ii</scp>) complexes: characterization details, theoretical studies, promising enzyme-like activities, and biomolecular interactions
Subrata Mandal, Rahul Naskar, Apurba Sau Mondal, Biswajit Bera, Tapan Kumar Mondal
Abstract
) of the complexes with the protein. They actively suppressed the protein's intrinsic fluorescence in a static quenching mode, as further determined by fluorescence lifetime titration of protein with the complexes. Circular dichroism and synchronous spectroscopic experiments supported the protein's conformational alterations mediated by copper(II) complexes (1-3) in the microenvironment of the tryptophan residue of the protein. The typical binding distance between BSA and complexes was also computed using fluorescence resonance energy transfer. Of the three complexes (1-3), complex 3 stands out as the most efficacious.
Topics & Concepts
ChemistryLigand (biochemistry)CopperTitrationMetalAcetonitrileCrystallographyCoordination sphereStereochemistryInorganic chemistryCrystal structureOrganic chemistryBiochemistryReceptorMetal complexes synthesis and propertiesMetal-Catalyzed Oxygenation MechanismsCrystal structures of chemical compounds