Proton and phosphorus-31 NMR study of the dependence of diadenosine tetraphosphate conformation on metal ions

N. H. Kolodny, L. J. Collins

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

Adenosine 5'-tetraphospho-5'-adenosine (Ap 4A) plays a role in cellular metabolism in a wide variety of organisms. Because the divalent cations Mg 2+ and Zn 2+ are involved in the synthesis and function of Ap 4A, the effect of divalent cations on the dinucleotide's conformation is of interest. 1H and 31P chemical shift experiments were carried out as a function of Mg 2+ concentration and pH. We propose that Mg 2+ stabilizes the unusual ring-stacked conformation of Ap 4A at pH > 2 by interacting with the β-phosphates. To further probe conformational effects, stable complexes of Ap 4A with Co 3+ were studied using 1H and 31P NMR. Co 3+ forms two different bidentate complexes with Ap 4A, independent of whether the other four octahedral coordination sites are occupied by ammonia or trimethylenediamine. NMR results suggest that in one complex the Co 3+ is coordinated to two β-phosphates and ring stacking is stabilized. In the other complex, Co 3+ is coordinated to an α-phosphate and its neighboring β-phosphate and ring stacking is destabilized. These results further support the hypothesis that Mg 2+ stabilizes the ring-stacked conformation by interacting symmetrically with the two β-phosphate groups.

Original languageEnglish (US)
Pages (from-to)14571-14575
Number of pages5
JournalJournal of Biological Chemistry
Volume261
Issue number31
StatePublished - 1986

Fingerprint

Phosphorus
Metal ions
Conformations
Protons
Metals
Phosphates
Nuclear magnetic resonance
Ions
Divalent Cations
Chemical shift
Ammonia
Metabolism
diadenosine tetraphosphate
Experiments

ASJC Scopus subject areas

  • Biochemistry

Cite this

Proton and phosphorus-31 NMR study of the dependence of diadenosine tetraphosphate conformation on metal ions. / Kolodny, N. H.; Collins, L. J.

In: Journal of Biological Chemistry, Vol. 261, No. 31, 1986, p. 14571-14575.

Research output: Contribution to journalArticle

@article{03638c8d9bf4409ea65794c41a1048f2,
title = "Proton and phosphorus-31 NMR study of the dependence of diadenosine tetraphosphate conformation on metal ions",
abstract = "Adenosine 5'-tetraphospho-5'-adenosine (Ap 4A) plays a role in cellular metabolism in a wide variety of organisms. Because the divalent cations Mg 2+ and Zn 2+ are involved in the synthesis and function of Ap 4A, the effect of divalent cations on the dinucleotide's conformation is of interest. 1H and 31P chemical shift experiments were carried out as a function of Mg 2+ concentration and pH. We propose that Mg 2+ stabilizes the unusual ring-stacked conformation of Ap 4A at pH > 2 by interacting with the β-phosphates. To further probe conformational effects, stable complexes of Ap 4A with Co 3+ were studied using 1H and 31P NMR. Co 3+ forms two different bidentate complexes with Ap 4A, independent of whether the other four octahedral coordination sites are occupied by ammonia or trimethylenediamine. NMR results suggest that in one complex the Co 3+ is coordinated to two β-phosphates and ring stacking is stabilized. In the other complex, Co 3+ is coordinated to an α-phosphate and its neighboring β-phosphate and ring stacking is destabilized. These results further support the hypothesis that Mg 2+ stabilizes the ring-stacked conformation by interacting symmetrically with the two β-phosphate groups.",
author = "Kolodny, {N. H.} and Collins, {L. J.}",
year = "1986",
language = "English (US)",
volume = "261",
pages = "14571--14575",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "31",

}

TY - JOUR

T1 - Proton and phosphorus-31 NMR study of the dependence of diadenosine tetraphosphate conformation on metal ions

AU - Kolodny, N. H.

AU - Collins, L. J.

PY - 1986

Y1 - 1986

N2 - Adenosine 5'-tetraphospho-5'-adenosine (Ap 4A) plays a role in cellular metabolism in a wide variety of organisms. Because the divalent cations Mg 2+ and Zn 2+ are involved in the synthesis and function of Ap 4A, the effect of divalent cations on the dinucleotide's conformation is of interest. 1H and 31P chemical shift experiments were carried out as a function of Mg 2+ concentration and pH. We propose that Mg 2+ stabilizes the unusual ring-stacked conformation of Ap 4A at pH > 2 by interacting with the β-phosphates. To further probe conformational effects, stable complexes of Ap 4A with Co 3+ were studied using 1H and 31P NMR. Co 3+ forms two different bidentate complexes with Ap 4A, independent of whether the other four octahedral coordination sites are occupied by ammonia or trimethylenediamine. NMR results suggest that in one complex the Co 3+ is coordinated to two β-phosphates and ring stacking is stabilized. In the other complex, Co 3+ is coordinated to an α-phosphate and its neighboring β-phosphate and ring stacking is destabilized. These results further support the hypothesis that Mg 2+ stabilizes the ring-stacked conformation by interacting symmetrically with the two β-phosphate groups.

AB - Adenosine 5'-tetraphospho-5'-adenosine (Ap 4A) plays a role in cellular metabolism in a wide variety of organisms. Because the divalent cations Mg 2+ and Zn 2+ are involved in the synthesis and function of Ap 4A, the effect of divalent cations on the dinucleotide's conformation is of interest. 1H and 31P chemical shift experiments were carried out as a function of Mg 2+ concentration and pH. We propose that Mg 2+ stabilizes the unusual ring-stacked conformation of Ap 4A at pH > 2 by interacting with the β-phosphates. To further probe conformational effects, stable complexes of Ap 4A with Co 3+ were studied using 1H and 31P NMR. Co 3+ forms two different bidentate complexes with Ap 4A, independent of whether the other four octahedral coordination sites are occupied by ammonia or trimethylenediamine. NMR results suggest that in one complex the Co 3+ is coordinated to two β-phosphates and ring stacking is stabilized. In the other complex, Co 3+ is coordinated to an α-phosphate and its neighboring β-phosphate and ring stacking is destabilized. These results further support the hypothesis that Mg 2+ stabilizes the ring-stacked conformation by interacting symmetrically with the two β-phosphate groups.

UR - http://www.scopus.com/inward/record.url?scp=0022855851&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0022855851&partnerID=8YFLogxK

M3 - Article

C2 - 3021745

AN - SCOPUS:0022855851

VL - 261

SP - 14571

EP - 14575

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 31

ER -