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• W2016172892 abstract "Potentiometric equilibrium studies of the system: glycylglycine–Zn(II)–OBISDIEN are described. Kinetic studies of hydrolysis and deuteration of glycylglycine catalyzed by dinuclear Zn(II)–OBISDIEN complexes have been carried out. The hydroxyl groups coordinated to the metal ion in the complex play an important role in the hydrolysis and deuteration reactions. The specific deuteration rate constants for individual species are kLZn2HP4+ (P=glycylglycine) and kLZn2P3+=0; kLZn2(OH)P2+=7.0×10−7 s−1; kLZn2(OH)2P+=42.5×10−7 s−1 and kLZn2(OH)3P+=42.5×10−7 s−1 also. The specific rate constants for the hydrolysis reaction are kLZn2HP4+ and kLZn2P3+≅1.0×10−7 s−1; kLZn2(OH)P2+=4.6×10−7 s−1; kLZn2(OH)2P+=4.8×10−7 s−1 and kLZn2(OH)3P+=4.9×10−7 s−1. The results show that the most active species toward hydrolysis are the hydroxo species. The hydroxide groups are bound to the metal centers in the cavity of OBISDIEN, and glycylglycine probably has its carboxylate group coordinated to the Zn2+ on one side and the amide carbonyl coordinated to the other Zn2+ at the other side of the macrocycle. The role of the hydroxide ion coordinated to the metal ion at the active center of hydrolytic enzymes seems to be important, and this model shows that the hydroxide ion coordinated to the metal center increases the rate constant of hydrolysis by an average of 4.8 times, and the hydroxo complexes are the only active species for the deuteration reactions." @default.
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• W2016172892 date "1999-04-01" @default.
• W2016172892 modified "2023-09-27" @default.
• W2016172892 title "Molecular recognition of dipeptides. Catalysis of deuteration and hydrolysis of glycylglycine by dinuclear OBISDIEN Zn(II) complexes" @default.
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• W2016172892 doi "https://doi.org/10.1016/s0020-1693(98)00416-2" @default.
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