Sodium binding to and protonation of ATP: a multinuclear magnetic double resonance study at 8.46 tesla

We show that the interaction of ATP with Na + and H +, whether binding of dissociation, gives rise to exchange broadened 31P-NMR spectra at 8.4 T, pH 6.7 and 310 K. We interpret the effect as being due to a two-step conversion between two NMR-differentiated ATP pools. A quantitative analysis yields...

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Published inBiochimica et biophysica acta Vol. 926; no. 1; pp. 106 - 113
Main Authors Pilatus, U., Mayer, A., Offermann, W., Leibfritz, D.
Format Journal Article
LanguageEnglish
Published Amsterdam Elsevier B.V 08.10.1987
Elsevier
North-Holland
Subjects
Adenosine Triphosphate
Analytical, structural and metabolic biochemistry
ATP protonation
Biological and medical sciences
Fundamental and applied biological sciences. Psychology
Inorganic compounds
Kinetics
Magnesium
Magnetic Resonance Spectroscopy - methods
NMR
Other biological molecules
Sodium
Sodium binding
Sodium Chloride
NMR
Sodium binding
ATP protonation
Equilibrium constant
Fixation
Sodium
Hydrogen
Molecular interaction
Dissociation
Nuclear magnetic resonance
ATP
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Summary:We show that the interaction of ATP with Na + and H +, whether binding of dissociation, gives rise to exchange broadened 31P-NMR spectra at 8.4 T, pH 6.7 and 310 K. We interpret the effect as being due to a two-step conversion between two NMR-differentiated ATP pools. A quantitative analysis yields all involved equilibrium constants and some of the dynamic parameters. Our results help to understand previous studies of magnesium binding to ATP and the appearance of high-field in vivo 31P-NMR spectra.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0304-4165
0006-3002
1872-8006
DOI:10.1016/0304-4165(87)90187-5