In this dissertation, Selectively recognize interaction has been studied between naphthalene imide derivatives and different anions and positive ions. There are two derivatives which can selectively recognize with ions. The coordinate constant has been obtained. On the basis of recognition, the influence of ATP hydrolysis catalyzed by the two ligands has also been studied. The hydrolysis rate constants catalysis by ligands show that there has more catalysis of ligand for ATP hydrolysis. The detail results were following:1A new compound, ammonia ethyl-N-1,8-naphthlene formyl imine(L1), was synthesized and characterized. Recognition interaction between L1and various anions and cations were detected by fluorescence spectrometry. L1can selectively recognize Ni2+and F", and the coordinate constant of L1and Ni2+was2.76×104L/mol. The quenching constant of Li by F-was1.65×105L/mol.2The interaction between L1and ATP has been studied by fluorescence titration experiment, the stability constant is3.21×104L/mol. Furthermore, the catalysis of ligand (L1) on ATP hydrolysis was also studied by molybdenum blue method. The optimum condition is50℃and pH value is6. The hydrolysis rate constant (Kobs) is5.99×10-2h-1.It is increased about2.55times comparing with the hydrolysis rate constants of ATP without the addition of L1,2.35×10-2h-1, in the same condition.3The other new compound,1,8-naphthalene diformate-L-histidine(L2), was synthesized and characterized. Recognition interaction between L2and various cations were detected by fluorescence spectrometry. L2can selectively recognize La3+ã€Cd2+ã€Ba2+and Zn2+. The coordinate constant of L2and La3+was1.25x106L/mol.4The interaction between L2and ATP has been studied by fluorescence titration experiment, the stability constant between L2and ATP is6.72×105L/mol. Furthermore, the catalysis of ligand (L2) on ATP hydrolysis was also studied by molybdenum blue method. The optimum condition is40℃and pH value is4. The hydrolysis rate constant (Kobs) is0.121811h-1. It is increased about11.70times comparing with the hydrolysis rate constants of ATP without the addition of L2,1.1041×10-2h-1, in the same condition. |