NMR evidence for Mg(II) binding to N1 of ATP.
The conformation of the complex of [ATP-Mg]2+ is studied by 1H, 15N and 31P NMR on ATP in the absence and presence of MgCl2 in a wide pH range from 1 to 10. 1H-15N HMBC experiments show a large change in the 15N chemical shift of N1 up to 10 ppm around pH 3.7, suggesting that there is a strong interaction between Mg2+ and N1 of ATP at this pH. 31P NMR indicates that at pH 3.7 the phosphate chain also binds Mg2+. 1H diffusion measurements imply that the [ATP-Mg]2+ complex involves only one ligand and one metal ion.
Jiang
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Laboratory of NMR and Atomic Molecular Physics, Wuhan Institute of Physics and Mathematics, The Chinese Academy of Sciences, Wuhan, People's Republic of China.
Mao
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D000255:Adenosine Triphosphate / Q000737:chemistry*; D008274:Magnesium / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D015394:Molecular Structure; D009587:Nitrogen Isotopes
D009587:Nitrogen Isotopes; D000255:Adenosine Triphosphate; D008274:Magnesium