高等学校化学学报 ›› 2002, Vol. 23 ›› Issue (5): 763.

• 研究论文 • 上一篇    下一篇

Cd(Ⅱ)和ATP的结合位点的NMR研究

姜凌, 毛希安   

  1. 中国科学院武汉物理与数学研究所, 波谱与原子分子物理国家重点实验室, 武汉 430071
  • 收稿日期:2001-06-13 出版日期:2002-05-24 发布日期:2002-05-24
  • 通讯作者: 毛希安(1952年出生),男,博士,研究员,从事核磁共振应用研究.
  • 基金资助:

    国家自然科学基金(批准号:29725307)资助.

NMR Study of ATP Binding Site with Cd2+

JIANG Ling, MAO Xi-An   

  1. State Key Laboratory of MR and Atomic &Molecular Physics, Wuhan Institute of Physics &Mathematics, Chinese Academy of Sciences, Wuhan 430071, China
  • Received:2001-06-13 Online:2002-05-24 Published:2002-05-24

摘要: 用NMR方法研究了金属镉离子在ATP(嘌呤三磷酸腺苷)上的配位点.测量了不同pH值时由于Cd2+的存在而引起的1H,15N及31P的化学位移和31P-31P中的偶合常数的变化以及由ATP的存在所引起的113Cd的化学位移的变化.结果表明,在pH>4.5的条件下,ATP主要以磷酸根和N7同时对Cd2+配位;在pH值2.5~4.5的条件下,ATP主要以磷酸根和N1同时对Cd2+配位,还存在少量的磷酸根和N7同时配位的模式;而在酸性非常强的条件下(pH<2.5),ATP不再与Cd2+相互作用。

关键词: ATP-Cd配合物, pH, 化学位移, 配位点

Abstract: In this paper, the binding site of Cd2+ at the purine ring of ATPwas studied by using NMRtechnique.The changes of :H, 15Nand 31Pchemical shifts and 31P-31Pcoupling constants due to the presence of Cd2+ and the change of 113Cd chemical shift due to the presence of ATPin a wide pHrange are measured.It is found that, when pH>4.5, ATPchelates Cd2+ with its phosphate and N7; at pH 2.5—4.5, ATP binding sites are mainly phosphate and Nl, but phosphate/N7 mode still exists; when pHis very low (pH<2.5), ATPdoes not interact with Cd2+.

Key words: ATP-Cd2+ complex, pH, Chemical shift, Binding site

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