Multiple interactions in Zn(II) ternary systems of phenanthroline bridging polyaza ligand and adenosine, 5’-triphosphate
Yanhe Guoa, Qingchun Gea, Hai Linb, Huakuan Lina* & Shourong Zhua
The stability of Zn(II) ternary complexes of phenanthroline bridging polyaza ligand and ATP have been determined using potentiometric pH titrations, 1H and 31P NMR spectra. Protonated metal complexes interact with the polyphosphate chain of the nucleotide substrate by coordination, electrostatic and H-bonding interactions, as well as stacking interactions between the phenanthroline moiety of L and the nucleoside residue of ATP. Moreover, ion--donor, hydrophobic and even van der Waals interactions may exist in the ternary systems. The recognition of nucleotides is promoted by adding Zn(II) to the receptor/ substrate system. Zn(II) acts as a “messenger” to bridge the polyamine and ATP, which in turn leads to the competition between the mixed ligands in binding zinc ion. Thus, the supramolecules formed by self-assembly are good models to mimic the active center of the ATPase.
Indian Journal of Chemistry
Vol. 42A, February 2003, pp 292-294
Yanhe Guoa, Qingchun Gea, Hai Linb, Huakuan Lina* & Shourong Zhua
The stability of Zn(II) ternary complexes of phenanthroline bridging polyaza ligand and ATP have been determined using potentiometric pH titrations, 1H and 31P NMR spectra. Protonated metal complexes interact with the polyphosphate chain of the nucleotide substrate by coordination, electrostatic and H-bonding interactions, as well as stacking interactions between the phenanthroline moiety of L and the nucleoside residue of ATP. Moreover, ion--donor, hydrophobic and even van der Waals interactions may exist in the ternary systems. The recognition of nucleotides is promoted by adding Zn(II) to the receptor/ substrate system. Zn(II) acts as a “messenger” to bridge the polyamine and ATP, which in turn leads to the competition between the mixed ligands in binding zinc ion. Thus, the supramolecules formed by self-assembly are good models to mimic the active center of the ATPase.
Indian Journal of Chemistry
Vol. 42A, February 2003, pp 292-294
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