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Complexes of Cu(II) ions and noncovalent interactions in systems with L-aspartic acid and cytidine-5'-monophosphate.
Bioinorganic Chemistry and Applications ( IF 3.8 ) Pub Date : 2008-01-01 , DOI: 10.1155/2008/253971
Romualda Bregier-Jarzebowska 1 , Anna Gasowska , Lechosław Lomozik
Affiliation  

Interactions between aspartic acid (Asp) and cytidine-5-monophosphate (CMP) in metal-free systems as well as the coordination of Cu(II) ions with the above ligands were studied. The composition and overall stability constants of the species formed in those systems were determined by the potentiometric method, and the interaction centres in the ligands were identified by the spectral methods UV-Vis, EPR, NMR, and IR. In metal-free systems, the formation of adducts, in which each ligand has both positive and negative reaction centres, was established. The main reaction centres in Asp are the oxygen atoms of carboxyl groups and the nitrogen atom of the amine group, while the main reaction centre in CMP at low pH is the N(3) atom. With increasing pH, the efficiency of the phosphate group of the nucleotide in the interactions significantly increases, and the efficiency of carboxyl groups in Asp decreases. The noncovalent reaction centres in the ligands are simultaneously the potential sites of metal-ion coordination. The mode of coordination in the complexes formed in the ternary systems was established. The sites of coordination depend clearly on the solution pH. In the molecular complexes MLcdots, three dots, centeredL, metallation involves the oxygen atoms of the carboxyl groups of the amino acid, while the protonated nucleotide is in the outer coordination sphere and interacts noncovalently with the anchoring CuH(x)(Asp) species. The influence of the metal ions on the weak interactions between the biomolecules was established.

中文翻译:

Cu(II) 离子的复合物和非共价相互作用在系统中与 L-天冬氨酸和胞苷-5'-单磷酸盐。

研究了无金属系统中天冬氨酸 (Asp) 和胞苷-5-单磷酸酯 (CMP) 之间的相互作用以及 Cu(II) 离子与上述配体的配位。在这些系统中形成的物质的组成和整体稳定性常数通过电位法确定,配体中的相互作用中心通过光谱方法 UV-Vis、EPR、NMR 和 IR 确定。在不含金属的系统中,形成了加合物,其中每个配体都有正负反应中心。Asp中的主要反应中心是羧基的氧原子和胺基的氮原子,而CMP在低pH下的主要反应中心是N(3)原子。随着 pH 值的增加,核苷酸的磷酸基团在相互作用中的效率显着增加,Asp中羧基的效率降低。配体中的非共价反应中心同时是金属离子配位的潜在位点。建立了三元体系中形成的配合物的配位模式。配位点显然取决于溶液的 pH 值。在分子复合物 MLcdots 中,三个以 L 为中心的点金属化涉及氨基酸羧基的氧原子,而质子化核苷酸位于外部配位球中,并与锚定的 CuH(x)(Asp) 物质非共价相互作用。确定了金属离子对生物分子间弱相互作用的影响。配体中的非共价反应中心同时是金属离子配位的潜在位点。建立了三元体系中形成的配合物的配位模式。配位点显然取决于溶液的 pH 值。在分子复合物 MLcdots 中,三个以 L 为中心的点金属化涉及氨基酸羧基的氧原子,而质子化核苷酸位于外部配位球中,并与锚定的 CuH(x)(Asp) 物质非共价相互作用。确定了金属离子对生物分子间弱相互作用的影响。配体中的非共价反应中心同时是金属离子配位的潜在位点。建立了三元体系中形成的配合物的配位模式。配位点显然取决于溶液的 pH 值。在分子复合物 MLcdots 中,三个以 L 为中心的点金属化涉及氨基酸羧基的氧原子,而质子化核苷酸位于外部配位球中,并与锚定的 CuH(x)(Asp) 物质非共价相互作用。确定了金属离子对生物分子间弱相互作用的影响。金属化涉及氨基酸羧基的氧原子,而质子化核苷酸位于外部配位球中并与锚定 CuH(x)(Asp) 物质非共价相互作用。确定了金属离子对生物分子间弱相互作用的影响。金属化涉及氨基酸羧基的氧原子,而质子化核苷酸位于外部配位球中并与锚定 CuH(x)(Asp) 物质非共价相互作用。确定了金属离子对生物分子间弱相互作用的影响。
更新日期:2019-11-01
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