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Beryllium(II) binding to ATP and ADP: Potentiometric determination of the thermodynamic constants and implications for in vivo toxicity

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Abstract

Highly toxic beryllium(II) is divalent metal ion with a high charge density, making it a potential target for binding to bio-molecules rich in O donor groups. In aqueous solution Be2+ binds to ATP and ADP to form 1:1 Be2+:ATP and Be2+:ADP complexes in relatively acidic media. At neutral pH the complex formed undergoes hydrolysis. Be2+ binding to ATP and ADP is much stronger than Ca2+ and Mg2+ binding. The high affinity of Be2+ toward ATP and ADP binding suggests a mechanism relevant to understanding the in vivo chemical toxicity of this metal.

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References

  • Bigelow DJ, Inesi G. 1992 Contributions of chemical derivatization and spectroscopic studies to the characterization of the calcium transport ATPase of sarcoplasmic reticulum. Biochim Biophys Acta 1113, 323-338.

    Google Scholar 

  • Bishop EO, Kimber SJ, Orchard D, Smith BE. 1981 A P-31 nmr study of mono-and dimagnesium complexes of adensosine 5'-triphosphate and model systems. Biochim Biophys Acta 635, 63-72.

    Google Scholar 

  • Campbell AM, Kessler PD, Sagara Y, Inesi G, Farbrough DM. 1991 Nucleotide sequences of avian cardiac and brain SR/ER Ca(2+)-ATPases and functional comparisons with fast twitch Ca(2+)-ATPase. Calcium affinities and inhibitor effects. J Biol Chem 266, 16050-16055.

    Google Scholar 

  • Hasselbach W, Makinose M. 1961 The calcium pump of the granules of the muscle and their dependence on adenosine triphosphate hydrolysis. Biochem Z 333, 518-528.

    Google Scholar 

  • Huang SL, Tsai M-D. 1962 Does the magnesium(II) ion interact with the α-phosphate of ATP? An investigation by oxygen-17 nuculear magnetic resonance. Biochemistry 21, 951-959.

    Google Scholar 

  • Inesi G, Kurzmack M, Lewis, D. 1988 Kinetic and equilibrium characterization of an energy-transducing enzyme and its partial reactions. Methods Enzymol 157, 154-190.

    Google Scholar 

  • Lewis JG, Gawdi G, Pizzo SV, Misra UK. 1999 Exposure of cultured macrophages to low concentrations of beryllium induces increases in intracellular calcium concentrations and stimulates DNA synthesis. J Leuk Biol 65, 786-791.

    Google Scholar 

  • MacLennan DH, Brandl CJ, Korczak B, Green NM. 1985 Aminoacid sequence of a Ca2+ + Mg2+-dependent ATPase from rabbit muscle sarcoplasmic reticulum, deduced from its complementary DNA sequence. Nature 316, 696-700.

    Google Scholar 

  • Martell AE, Smith RM. (1974-1982) Critical Stability Constants. Plenum Press: New York; Vols. 1-4.

    Google Scholar 

  • Phan B, Reisler E. 1992 Inhibition of myosin ATPase by beryllium fluoride. Biochemistry 31, 4787-4793.

    Google Scholar 

  • Sankaran B, Bhagat S, Senior AE. 1997 Inhibition of P-glycoprotein ATPase activity by beryllium fluoride. Biochemistry 36, 6847-6853.

    Google Scholar 

  • Shanbhag SM, Choppin GR. 1987 Thermodynamics of Mg and Ca complexation with AMP, ADP, ATP. Inorg Chim Acta 138, 187-192.

    Google Scholar 

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Correspondence to Alvin L. Crumbliss.

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Boukhalfa, H., Lewis, J.G. & Crumbliss, A.L. Beryllium(II) binding to ATP and ADP: Potentiometric determination of the thermodynamic constants and implications for in vivo toxicity. Biometals 17, 105–109 (2004). https://doi.org/10.1023/B:BIOM.0000018359.25658.9c

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  • DOI: https://doi.org/10.1023/B:BIOM.0000018359.25658.9c

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