The Concept of Phosphate Compounds of High and Low Energy

  • Leopoldo de Meis


Life requires that different forms of energy are continuously interconverted in the cell. For this purpose phosphate compounds are used as the common currency of energy exchange and adenosine triphosphate (ATP) is the principal carrier of energy in the living cell. The hydrolysis of ATP is usually coupled with work. This can be mechanical, as observed in muscle contraction, chemical, as for the synthesis of molecules or osmotic when a gradient is formed across a membrane. It has been shown that several processes of energy conversion are reversible. Thus, several membrane bond ATPase hydrolyze ATP in order to build up an ionic gradient across a membrane and in the reverse process, the energy derived from the gradient can be used to synthesize ATP from ADP and Pi


Sarcoplasmic Reticulum Water Activity Catalytic Site Creatine Phosphate Catalytic Cycle 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. Alberty, R.A. (1969). Standard Gibbs free energy, as a function of pH and pMg for reactions involving adenosine phosphates. J.Biol.Chem. 244: 3290–3302.PubMedGoogle Scholar
  2. Barlogie, B.. Hasselbach, W., & Makinose, M. (1971). Activation of calcium effux by ADP and inorganic phosphate. FEBS Lett. 12: 267–268.Google Scholar
  3. Boyd, D. B. & Lipscomb, W. N. (1969). Electronic Structures for Energy-Rich Phosphates. J.Theor.Biol. 25: 403–420.PubMedCrossRefGoogle Scholar
  4. Boyer, P.D., Ross, R.L., & Momsen, W. (1973). A new concept for coupling in oxidative phosphorylation based on the oxigen exchange reactions. Proc. Natl. Acad. Sci. USA 70: 2837–2839.Google Scholar
  5. Clarke, D.M., Loo, T.W., lnesi, G., & MacLennan, D.H. (1989). Location of high affinity Ca2+ binding sites within the predicted transmembrane domain of the sarcoplasmic reticulum Ca2+ ATPase. Nature 339: 476–478.PubMedCrossRefGoogle Scholar
  6. Cohen, I. Bernard. In Revolution in science, pp 229 236. The Belknap Press of Harvard University Press, Cambridge, Mass.Google Scholar
  7. Cooke, R., & Kuntz, I.D. (1974). The properties of water in biological systems. Annu.Rev.Biophys. Bioeng. 3: 95–107.Google Scholar
  8. Cori, G.T., Cori, C.F. & Schmidt, G. (1936). Mechanism of formation of hexosemonophosphate in muscle and isolation of a new phosphate ester. Proc.Soc. Exp. Biol. and Med. 34: 702–708.Google Scholar
  9. de Meis, L. (1984). Pyrophosphate of high and low energy: Contribution of pH, Ca2+, Mg2+ and water to free en¬ergy of hydrolysis. J. Biol. Chem. 259: 6090–6097.Google Scholar
  10. de Meis, L. (1989). Role of water in the energy of hydrolysis of phosphate compounds-Energy Transduction in Biological Membranes. Biochem. Biophys. Acta (Reviews) 973: 333–344.Google Scholar
  11. de Meis, L. (1993). The concept of energy-rich phosphate compounds: water, transport ATPases and entropie en¬ergy Arch. Biochem. Biophys. 306: 287–296.Google Scholar
  12. de Meis, L. Grieco, M.A., & Galina, A. (1992). Reversal of oxidative phosphorylation in submitochondrial parti¬cles using glucose 6-phosphate and hexokinase as an ATP regenerating system. FEBS Lett. 308: 197–201.Google Scholar
  13. de Meis, L., & Carvalho, M.G.C. (1974). Role of the Ca2+ concentration gradient in the adenosine 5’triphosphate. Inorganic phosphate exchange catalyzed by sarcoplasmic reticulum. Biochemistry 13: 5032–5038.Google Scholar
  14. de Meis, L., & Inesi, G. (1982). ATP synthesis by sarcoplasmic reticulum ATPase following Ca2+, pH temperature and water activity jumps. J. Biol. Chem. 257: 1289–1294.Google Scholar
  15. de Meis, L., & Inesi, G. (1985). Enzyme phosphorylation with Pi causes Ca2+ dissociation from sarcoplasmic reticulum ATPase. Biochemistry 24: 922–925.PubMedCrossRefGoogle Scholar
  16. de Meis, L., & Turne, R.K. (1977). A new mechanism by which and H concentration gradient drives the synthesis of ATP, pH jump, and ATP synthesis by the Ca2+ dependent ATPase of sarcoplasmic reticulum Biochemistry 16: 4455–4463.Google Scholar
  17. de Meis, L., & Vianna, A.L. (1979). Energy interconversion by the Ca2+ transport ATPase of sarcoplasmic reticulum. Annu.Rev.Biochem. 48: 275–292.PubMedCrossRefGoogle Scholar
  18. de Meis, L., Martins, O.B. & Alves, E.W. (1980). Role of water, hydrogen ions, and temperature on the synthesis of adenosine triphosphate by the sarcoplasmic reticulum Adenosine Tryphosphatase in the absence of a calcium ion gradient. Biochemistry 19: 4252–4261.PubMedCrossRefGoogle Scholar
  19. de Meis, L., Monteiro-Lomeli, M., Grieco, M.A., and Galina, A. (1992). The Maxwell Demon in Biological systems-Use of glucose 6-phosphate and hexokinase as an ATP regenerating system by the Ca2+ ATPase of sarcoplasmic reticulum and submitochondrial particles. Ann. N.Y. Acad. Sci. 671: 19–31.Google Scholar
  20. de Meis, L.,Behrens, M.I., Petretski, J.H., & Politi, M.J. (1985). Contribution of water to free energy of hydrolysis of pyrophosphate. Biochemistry 24: 7783–7789.Google Scholar
  21. Eggleton, P. & Eggleton, G.P. (1927). Inorganic phosphate and labile form of organic phosphate in gastrocnemius of frog. Biochem. J. 21: 190–194.Google Scholar
  22. Ewig, C.S. &Van Wazer, J.R. (1988). Ab Initio structures of phosphorus acids and esters. 3. The P-O-P Bridged compounds H4P,02n_1 for n=l to 4. J. Am. Chem. Soc. 110: 79–86.Google Scholar
  23. Fiske, C.H. & Subbarow, Y. (1925) The colorometric determination of phosphorus. J. Biol. Chem. 66:375–381. Fiske, C.H. and Subbarow, Y. (1927). The nature of the “inorganic phosphate” in voluntary muscle. Science 65: 401.Google Scholar
  24. Fiske, C.H. & Subbarow, Y. (1929). Phosphorus compounds of muscle and liver. J.Biol.Chem. 81: 629–635.Google Scholar
  25. Flodgaard, H., &Fleron, P. (1974). Termodynamic parameters for the hydrolysis of inorganic phosphate at pH 7.4 as a function of [Mg2+], [K+], and ionic strength determined from equilibrium studies of the reaction. J.Biol.Chem. 249: 3465–3474.PubMedGoogle Scholar
  26. George, P., Witonsky, R.J., Trachtman, M.. Wu, C., Dorwatr,W., Richman, L., Richman, W., Shuray, F. & Lentz, B. (1970) An enquiry into the importance of solvation effects in phosphate ester and anhydride reactions. Biochim.Biophys.Acta 223: 1–15.Google Scholar
  27. Hayes, M.D., Kenyon, L.G., and Kollman, A.P. (1978). Theoretical calculations of the hydrolysis energies of some “high-energy” molecules. J.Am.Chem.Soc. 100: 4331–4340.CrossRefGoogle Scholar
  28. Hill, T.L. & Morales, M.H. (1951). On ‘High Energy Phosphate Bonds’ of Biochemical Interest. J.Am.Chem.Soc. 73: 1656–1660.CrossRefGoogle Scholar
  29. Kalckar,M. (1941). An activator of the hexokinase system. J. Biol.Chem. 137: 789–790.Google Scholar
  30. Lipmann, F. (1941) Metabolic Generation and utilization of phosphate bond energy. Advances in Enzymology 1: 99–162.Google Scholar
  31. Lohmann,K. (1929). The chemistry of muscle contraction. Naturwiss. 17: 624–626.Google Scholar
  32. Lohmann,K. (1934). The chemistry of muscle contraction. Naturwiss. 22: 409–411.CrossRefGoogle Scholar
  33. Lundsgaard, E. (1932). The significant of the phonomenon “alactacid muscle contractions” for an interpretation of the chemistry of muscle contraction. Danske Hospitalstidennde, 75: 84–87.Google Scholar
  34. Makinose, M., & Hasselbach, W. (1971). ATP synthesis by the reverse of the sarcoplasmic reticulum pump. FEBS Lett. 12: 271–272.PubMedCrossRefGoogle Scholar
  35. Masuda, H., & de Meis, L. (1973). Phosphorylation of the sarcoplasmic reticulum membrane by orthophosphate. Inhibition by calcium ions. Biochemistry. 12: 4581–4585.Google Scholar
  36. Meyerhof, O. (1930). Conversion of fermentable hexoses with a yeast catalyst. (hexokinase). J.Springer, Berlin, pp. 149–155.Google Scholar
  37. Mitchell, P. (1961). Coupling of phosphorylation to electron and hydrogen transfer by a chemiosmotic type of mechanism. Nature 191: 144–148.PubMedCrossRefGoogle Scholar
  38. Montero-Lomeli, M., & de Meis, L. (1992). Glucose-6-phosphate and hexokinase can be used as an ATP regenerating system by the Ca2+ ATPase of Sarcoplasmic Reticulum. J. Biol. Chem. 267: 1829–1833.Google Scholar
  39. Moore, Walter J. (1962) Physical Chemistry. Prentice-Hall Inc., Englewood Cliffs, N.J. The Overthrow of the Phlogiston Theory. Harvard Case Histories in Experimental Sciences, J.B.Conant, ed. Harvard University Press, Cambridge, Mass.Google Scholar
  40. Pedersen, PL., & Carafoli, E. (1987). II. Energy coupling and work output. Trends Biochem. Sci. 12: 145–147.Google Scholar
  41. Pedersen, P.L., & Carafoli. E. (1987). Ion motive ATPases. I. Ubiquiti, properties, and significance to cell function. Trends Biochem. Sci. 12: 145.Google Scholar
  42. Penefsky, H.S., & Cross, R.L. (1991). Structure and mechanism of F11Fi-type ATP syntases and ATPases. Adv. Enzymol. Relat. Areas Mol. Biol. 64: 174–214.Google Scholar
  43. Romero, P., & de Meis, L. (1989). Role of water in the energy of hidrolysis of phospho-anhydride and phosphoesters bonds. J. Biol. Chem. 264: 7869–7873.Google Scholar
  44. Saenger, W. (1987). Structure and dynamics of mater surrounding biomolecules. Annu. Rev.Biophys. Biophys. Chem. 16: 93–102.Google Scholar
  45. Schlenk, F. (1985) Early research on fermentation-a story of missed opportunities. TIBS 10: 252.Google Scholar
  46. Schlenk, F. (1987). The ancestry, birth and adolescence of adenosine triphosphate. TIBS 12: 367–368.Google Scholar
  47. Srivastava, D.K., & Bernhard, S.A. (1987). Biophysical chemistry of metabolic reaction sequences in concentrated enzyme solution and in the cell. Annu. Rev. Biophys. Biophys. Chem. 16: 175–187.Google Scholar
  48. Tanford, C. (1984). Twenty questions concerning the reaction cycle of the Sarcoplasmic Reticulum calcium pump. Crit. Rev. Biochem. 17: 123–151.Google Scholar
  49. Wilkinson, K.D., & Rose, I.A. (1979). Activation of yeast hexokinase PII. Changes in conformation and association. J. Biol. Chem. 254: 2125–2129.Google Scholar
  50. Wolfenden, R., & Williams, R. (1985). Solvent water and the biological group-transfer potential of phosphoric and carboxylic anhydrides. J. Am. Chem. Soc. 107: 4345–4346.Google Scholar

Copyright information

© Springer Science+Business Media New York 1997

Authors and Affiliations

  • Leopoldo de Meis
    • 1
  1. 1.Instituto de Ciências Biomedicas Departamento de Bioquímica MedicaUniversidade Federal do Rio de JaneiroRio de JaneiroBrazil

Personalised recommendations