Ap4A is not an efficient Zn(II) binding agent. A concerted potentiometric, calorimetric and NMR study

Małgorzata Wszelaka-Rylik; Aleksandra Witkiewicz-Kucharczyk; Jacek Wójcik; Wojciech Bal

doi:10.1016/j.jinorgbio.2007.01.007

Ap4A is not an efficient Zn(II) binding agent. A concerted potentiometric, calorimetric and NMR study

J Inorg Biochem. 2007 May;101(5):758-63. doi: 10.1016/j.jinorgbio.2007.01.007. Epub 2007 Jan 30.

Authors

Małgorzata Wszelaka-Rylik¹, Aleksandra Witkiewicz-Kucharczyk, Jacek Wójcik, Wojciech Bal

Affiliation

¹ Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawińskiego 5a, 02-106 Warsaw, Poland.

PMID: 17336388
DOI: 10.1016/j.jinorgbio.2007.01.007

Abstract

Diadenosine 5',5''-P(1)P(4) tetraphosphate (Ap(4)A) has been considered as an intracellular partner for Zn(II). We applied potentiometry, ITC and NMR to study protonation equilibria of Ap(4)A and Zn(II) complexation by this dinucleotide. The values of binding constants obtained by these three techniques under various experimental conditions coherently demonstrated that Ap(4)A binds Zn(II) weakly, with an apparent binding constant of ca. 10(4) at neutral pH. Such a low stability of Zn(II) complexes with Ap(4)A excludes a possibility for interactions between these two agents in vivo.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Calorimetry
Chlorides / chemistry*
Dinucleoside Phosphates / chemistry*
Magnetic Resonance Spectroscopy
Potentiometry
Zinc Compounds / chemistry*

Substances

Chlorides
Dinucleoside Phosphates
Zinc Compounds
diadenosine tetraphosphate
zinc chloride