25Mg NMR Studies of magnesium binding to erythrocyte constituents

Jay L. Bock, George B. Crull, Arnold Wishnia, Charles Jr Springer

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

The binding of Mg2+ ion to ATP, ADP, AMP, 2,3-bisphosphyoglycerate (DPG), and hemoglobin has been studied by 25Mg NMR spectroscopy at 9.4 T. Addition of any of these ligands to a solution of 2 mM25MgCl at pH 7.2 caused a progressive increase in linewidth, with no discernible chemical shift. ATP and ADP, which form tight 1:1 complexes with Mg2+, did not cause maximal broadening until present in several-fold excess, implying that bis(nucleotide) complexes also form. The studies showed progressively weaker Mg2+ binding to ATP, ADP, DPG, and AMP, consistent with published binding constants. Hemoglobin cause fairly little broadening, consistent with its known weak affinity for Mg2+. Competition studies determined ATP affinities for Ca2+ and H+ that were also in good agreement with published values. 25Mg NMR spectra of 2 mM bound 25Mg2+ were obtained with good signal to noise in less than 1 hr. The technique may now be a practical means for studying the binding of Mg2+ within erythrocytes and other cells.

Original languageEnglish (US)
Pages (from-to)79-87
Number of pages9
JournalJournal of Inorganic Biochemistry
Volume44
Issue number2
DOIs
StatePublished - Nov 1 1991
Externally publishedYes

Fingerprint

Magnesium
Adenosine Triphosphate
Erythrocytes
Nuclear magnetic resonance
Adenosine Diphosphate
Adenosine Monophosphate
Hemoglobins
2,3-Diphosphoglycerate
Chemical shift
Linewidth
Nuclear magnetic resonance spectroscopy
Noise
Magnetic Resonance Spectroscopy
Nucleotides
Ions
Ligands

ASJC Scopus subject areas

  • Biochemistry
  • Inorganic Chemistry

Cite this

25Mg NMR Studies of magnesium binding to erythrocyte constituents. / Bock, Jay L.; Crull, George B.; Wishnia, Arnold; Springer, Charles Jr.

In: Journal of Inorganic Biochemistry, Vol. 44, No. 2, 01.11.1991, p. 79-87.

Research output: Contribution to journalArticle

Bock, Jay L. ; Crull, George B. ; Wishnia, Arnold ; Springer, Charles Jr. / 25Mg NMR Studies of magnesium binding to erythrocyte constituents. In: Journal of Inorganic Biochemistry. 1991 ; Vol. 44, No. 2. pp. 79-87.
@article{e4419579a40b48b48c83a87a0dd07770,
title = "25Mg NMR Studies of magnesium binding to erythrocyte constituents",
abstract = "The binding of Mg2+ ion to ATP, ADP, AMP, 2,3-bisphosphyoglycerate (DPG), and hemoglobin has been studied by 25Mg NMR spectroscopy at 9.4 T. Addition of any of these ligands to a solution of 2 mM25MgCl at pH 7.2 caused a progressive increase in linewidth, with no discernible chemical shift. ATP and ADP, which form tight 1:1 complexes with Mg2+, did not cause maximal broadening until present in several-fold excess, implying that bis(nucleotide) complexes also form. The studies showed progressively weaker Mg2+ binding to ATP, ADP, DPG, and AMP, consistent with published binding constants. Hemoglobin cause fairly little broadening, consistent with its known weak affinity for Mg2+. Competition studies determined ATP affinities for Ca2+ and H+ that were also in good agreement with published values. 25Mg NMR spectra of 2 mM bound 25Mg2+ were obtained with good signal to noise in less than 1 hr. The technique may now be a practical means for studying the binding of Mg2+ within erythrocytes and other cells.",
author = "Bock, {Jay L.} and Crull, {George B.} and Arnold Wishnia and Springer, {Charles Jr}",
year = "1991",
month = "11",
day = "1",
doi = "10.1016/0162-0134(91)84020-A",
language = "English (US)",
volume = "44",
pages = "79--87",
journal = "Journal of Inorganic Biochemistry",
issn = "0162-0134",
publisher = "Elsevier Inc.",
number = "2",

}

TY - JOUR

T1 - 25Mg NMR Studies of magnesium binding to erythrocyte constituents

AU - Bock, Jay L.

AU - Crull, George B.

AU - Wishnia, Arnold

AU - Springer, Charles Jr

PY - 1991/11/1

Y1 - 1991/11/1

N2 - The binding of Mg2+ ion to ATP, ADP, AMP, 2,3-bisphosphyoglycerate (DPG), and hemoglobin has been studied by 25Mg NMR spectroscopy at 9.4 T. Addition of any of these ligands to a solution of 2 mM25MgCl at pH 7.2 caused a progressive increase in linewidth, with no discernible chemical shift. ATP and ADP, which form tight 1:1 complexes with Mg2+, did not cause maximal broadening until present in several-fold excess, implying that bis(nucleotide) complexes also form. The studies showed progressively weaker Mg2+ binding to ATP, ADP, DPG, and AMP, consistent with published binding constants. Hemoglobin cause fairly little broadening, consistent with its known weak affinity for Mg2+. Competition studies determined ATP affinities for Ca2+ and H+ that were also in good agreement with published values. 25Mg NMR spectra of 2 mM bound 25Mg2+ were obtained with good signal to noise in less than 1 hr. The technique may now be a practical means for studying the binding of Mg2+ within erythrocytes and other cells.

AB - The binding of Mg2+ ion to ATP, ADP, AMP, 2,3-bisphosphyoglycerate (DPG), and hemoglobin has been studied by 25Mg NMR spectroscopy at 9.4 T. Addition of any of these ligands to a solution of 2 mM25MgCl at pH 7.2 caused a progressive increase in linewidth, with no discernible chemical shift. ATP and ADP, which form tight 1:1 complexes with Mg2+, did not cause maximal broadening until present in several-fold excess, implying that bis(nucleotide) complexes also form. The studies showed progressively weaker Mg2+ binding to ATP, ADP, DPG, and AMP, consistent with published binding constants. Hemoglobin cause fairly little broadening, consistent with its known weak affinity for Mg2+. Competition studies determined ATP affinities for Ca2+ and H+ that were also in good agreement with published values. 25Mg NMR spectra of 2 mM bound 25Mg2+ were obtained with good signal to noise in less than 1 hr. The technique may now be a practical means for studying the binding of Mg2+ within erythrocytes and other cells.

UR - http://www.scopus.com/inward/record.url?scp=0025918443&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0025918443&partnerID=8YFLogxK

U2 - 10.1016/0162-0134(91)84020-A

DO - 10.1016/0162-0134(91)84020-A

M3 - Article

C2 - 1787415

AN - SCOPUS:0025918443

VL - 44

SP - 79

EP - 87

JO - Journal of Inorganic Biochemistry

JF - Journal of Inorganic Biochemistry

SN - 0162-0134

IS - 2

ER -