A(p4)A is not an efficient Zn(II) binding agent. A concerted potentiometric, calorimetric and NMR study

作者：Wszelaka Rylik Malgorzata; Witkiewicz Kucharczyk Aleksandra; Wojcik Jacek; Bal Wojciech^*

来源：Journal of Inorganic Biochemistry, 2007, 101(5): 758-763.

DOI：10.1016/j.jinorgbio.2007.01.007

• A(P4)A
• Zn(II)
• stability constants
• potentiometry
• ITC
• NMR

Diadenosine 5',5"-(PP4)-P-1 tetraphosphate (ANA) has been considered as an intracellular partner for Zn(II). We applied potentiometry, ITC and NMR to study protonation equilibria of ANA 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.

• 出版日期2007-5