Binding site of Zn2+ in ATP:N1 at low pH and N7 at high pH as evidenced by 1H-15N NMR HMBC experiments

被引:15
作者
Du, F
Mao, XA
机构
[1] Chinese Acad Sci, Wuhan Inst Phys & Math, Lab Magnet Resonance & Atom Mol Phys, Wuhan 430071, Peoples R China
[2] Univ N Carolina, Dept Chem, Chapel Hill, NC 27599 USA
基金
中国国家自然科学基金;
关键词
zinc; abundant adenosine-5 '-triphosphate; binding site; pH; heteronuclear multiple bond correlation;
D O I
10.1016/S1386-1425(00)00286-9
中图分类号
O433 [光谱学];
学科分类号
0703 ; 070302 ;
摘要
Nuclear magnetic resonance (NMR) H-1-N-15 heteronuclear multiple bond correlation (HMBC) experiments on natural abundant adenosine-5'-triphosphate (ATP) showed that zinc(II) induced large chemical shifts (> 10 ppm) for N1 at lower pH (2-5) while for N7 at higher pH (5-7), suggesting that the binding site of Zn2+ in the purine base of ATP is pH dependent. The size effect of zinc(II) in coordination is also discussed. (C) 2000 Elsevier Science B.V. All rights reserved.
引用
收藏
页码:2391 / 2395
页数:5
相关论文
共 13 条
[11]   ISOMERIC EQUILIBRIA IN COMPLEXES OF ADENOSINE 5'-TRIPHOSPHATE WITH DIVALENT METAL-IONS - SOLUTION STRUCTURES OF M(ATP)2-COMPLEXES [J].
SIGEL, H .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1987, 165 (01) :65-72
[13]   Stabilities and structures of metal ion complexes of adenosine 5'-O-thiomonophosphate (AMPS(2-)) in comparison with those of its parent nucleotide (AMP(2-)) in aqueous solution [J].
Sigel, RKO ;
Song, B ;
Sigel, H .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1997, 119 (04) :744-755