Du F, Mao X A
Laboratory of Magnetic Resonance and Atomic Molecular Physics, Wuhan Institute of Physics and Mathematics, The Chinese Academy of Sciences, People's Republic of China.
Spectrochim Acta A Mol Biomol Spectrosc. 2000 Nov 1;56A(12):2391-5. doi: 10.1016/s1386-1425(00)00286-9.
Nuclear magnetic resonance (NMR) 1H-15N 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.
对天然丰度的腺苷 - 5'-三磷酸（ATP）进行的核磁共振（NMR）1H - 15N 异核多键相关（HMBC）实验表明，在较低pH值（2 - 5）时，锌（II）会使N1产生较大的化学位移（> 10 ppm），而在较高pH值（5 - 7）时会使N7产生较大化学位移，这表明ATP嘌呤碱基中Zn2 + 的结合位点依赖于pH值。同时还讨论了锌（II）配位中的尺寸效应。
