Zinc forms complexes with higher kinetical stability than calcium, 5-F-BAPTA as a good example

P. Csermely, Péter Sándor, Lajos Radics, János Somogyi

Research output: Contribution to journalArticle

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Abstract

Increasing interest is focused on the role of zinc in biological systems. A rapidly growing family of DNA-binding proteins contains "zinc-fingers", where zinc is bound to cysteine or histidine residues. On the other hand zinc is able to displace calcium from its binding sites and in this way it may modify calcium-mediated cellular processes. In the present report dissociation rates of Zn2+- and Ca2+-complexes with 5-F-BAPTA, a widely used NMR-active calcium indicator, have been measured by two-dimensional 19F NMR exchange spectroscopic methods. The results show that the lifetime of the Zn2+-complex is more than five times longer than that of the Ca2+-complex. The longer lifetime, when combined with a higher thermodynamical stability of the Zn2+-complex, may explain why, in some cellular processes, Zn2+ can compete with Ca2+ in spite of a presumably high [Ca2+]/[Zn2+] free ion concentration ratio.

Original languageEnglish
Pages (from-to)838-844
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume165
Issue number2
DOIs
Publication statusPublished - Dec 15 1989

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Zinc
Calcium
Zinc Fingers
Nuclear magnetic resonance
DNA-Binding Proteins
Histidine
Cysteine
Biological systems
Binding Sites
Ions
1,2-bis(2-aminophenoxy)ethane-N,N,N',N'-tetraacetic acid

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Zinc forms complexes with higher kinetical stability than calcium, 5-F-BAPTA as a good example. / Csermely, P.; Sándor, Péter; Radics, Lajos; Somogyi, János.

In: Biochemical and Biophysical Research Communications, Vol. 165, No. 2, 15.12.1989, p. 838-844.

Research output: Contribution to journalArticle

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