The Energetics of Active Transport

  • W. D. Stein


This chapter aims to give an overview of the workings of active-transport systems. I shall not go much into the details of any particular transport system—these will be the subjects of later chapters of this treatise—but I shall want to present what seem to me to be the general principles involved in the coupling between two flows of transported substrates or the coupling between the flow of a transported substrate and the progress of the chemical reaction that drives this flow. The standpoint adopted in this chapter is that such coupling, and, hence, active transport itself, arises simply from the properties of the membrane carriers, and, in particular, that such carriers, by virtue of their role as carriers, exist in two conformations facing the two sides of the cell membrane. It is the redistribution of carrier between its two major forms that brings about transport and active transport. The study of active transport is, then, the exploration of the properties of membrane-carrier systems. I shall work step-by-step through the principles of ligand-carrier interactions, transport on the simple carrier, active transport by countertransport, and, finally, active transport by cotransport, and in this way succeed, I hope, in showing that a sound knowledge of carrier kinetics provides the basis for an understanding of active transport. Much has been written on the energetics of active transport, on the interaction between the driving and the driven substrates, on the conformational energetics of the transporters, and on the possible role of high-energy chemical substrates in active transport. But an emphasis on the simple carrier basis of active transport may provide a newer way of looking at these old problems.


Active Transport Conformation Change Apparent Affinity Cytoplasmic Face Unidirectional Flux 
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. Cabantchik, Z. I., and Ginsburg, H., 1977, Transport of uridine in human red cells: Demonstration of a simple carrier-mediated process, J. Gen. Physiol. 69: 75–96.PubMedCrossRefGoogle Scholar
  2. Cleland, W. W., 1977, Determining the chemical mechanisms of enzyme-catalysed reactions by kinetic studies, Adv. Enzymol. 45: 273–387.PubMedGoogle Scholar
  3. Crane, R. K., 1977, The gradient hypothesis and other models of mediated active transport, Rev. Physiol. Biochem. Pharmacol. 78: 99–159.PubMedCrossRefGoogle Scholar
  4. Devés, R., and Krupka, R. M., 1981, Evidence for a two-state mobile camer mechanism in erythrocyte choline transport: Effects of substrate analogs on inactivation of the carrier by N-ethylmaleimide, J. Membr. Biol. 61: 21–30.PubMedCrossRefGoogle Scholar
  5. Glynn, I. M., 1985, The Nat, K+-transporting adenosine triphosphate, in: The Enzymes of Biological Membranes, Vol. 3 ( A. N. Martonosi, ed.), Plenum Press, New York, pp. 35–114.Google Scholar
  6. Glynn, I. M., and Karlish, S. J. D., 1982, Conformational changes associated with K’ transport by the Na+/K+-ATPase, in: Membranes and Transport (A. N. Martonosi, ed.), Plenum Press, New York, pp. 529–536.Google Scholar
  7. Holman, G. D., 1978, Cyclic AMP transport in human erythrocyte ghosts, Biochim. Biophys. Acta 508: 174–183.PubMedCrossRefGoogle Scholar
  8. Hopfer, U., and Groseclose, R., 1980, The mechanism of Nat-dependent D-glucose transport, J. Biol. Chem. 255: 4453–4462.PubMedGoogle Scholar
  9. Jencks, W. P., 1980, The utilization of binding energy in coupled vectorial processes, Adv. Enzymol. 51: 75–106.PubMedGoogle Scholar
  10. Karlish, S. J. D., 1980, Characterisation of conformational states in (Na,K)-ATPase labeled with fluorescein at the active site, J. Bioenerg. Biomembr. 12: 111–136.PubMedCrossRefGoogle Scholar
  11. Karlish, S. J. D., and Pick, U., 1981, Sidedness of the effects of sodium and potassium ions on the conformational state of the sodium—potassium pump, J. Physiol. (London) 312: 505–529.Google Scholar
  12. Karlish, S. J. D., and Yates, D. W., 1978, Tryptophan fluorescence of (Na` + K+)-ATPase as a tool for study of the enzyme mechanism, Biochim. Biophys. Acta 527: 111–130.Google Scholar
  13. Karlish, S. J. D., Lieb, W. R., and Stein, W. D., 1982, Combined effects of ATP and phosphate on rubidium–rubidium exchange mediated by Na-K-ATPase reconstituted into phospholipid vesicles, J. Physiol. (London) 328: 333–350.Google Scholar
  14. Klingenberg, M., 1985, The ADP/ATP carrier in mitochondrial membranes, in: The Enzymes of Biological Membranes, Vol. 4 ( A. N. Martonosi, ed.), Plenum Press, New York, pp. 511–553.Google Scholar
  15. Krupka, R. M., and Devés, R., 1979, The membrane valve: A consequence of asymmetrical inhibition of membrane carriers, Biochim. Biophys. Acta 550: 77–91.PubMedCrossRefGoogle Scholar
  16. Lieb, W. R., 1982, A kinetic approach to transport studies, in: Red Cell Membranes —A Methodological Approach (J. C. Ellory and J. D. Young, eds.), Academic Press, London, pp. 135–164.Google Scholar
  17. Mitchell, P., 1957, A general theory of membrane transport from studies of bacteria, Nature 180: 134–136.PubMedCrossRefGoogle Scholar
  18. Plagemann, P. G. W., Wohlhueter, R. H., and Erbe, J., 1982, Nucleoside transport in human erythrocytes: A simple carrier with directional symmetry and differential mobility of loaded and empty carrier, J. Biol. Chem. 257: 12069–12074.PubMedGoogle Scholar
  19. Rosenberg, R., 1981, L-leucine transport in human red blood cells: A detailed kinetic analysis, J. Membr. Biol. 62: 79–93.PubMedCrossRefGoogle Scholar
  20. Stein, W. D., 1981, Concepts of mediated transport, in: Membrane Transport, Chap. V ( S. L. Bonting and J. J. H. H. M. de Pont, eds.), Elsevier, Amsterdam, pp. 123–157.CrossRefGoogle Scholar
  21. Stein, W. D., and Lieb, W. R., 1973, A necessary simplification of the kinetics of carrier transport, Israel J. Chem. 11: 325–339.Google Scholar
  22. Tanford, C., 1982, Simple model for the chemical potential change of a transported ion in active transport, Proc. Natl. Acad. Sci. USA 79: 2882–2884.PubMedCrossRefGoogle Scholar
  23. Weber, G., 1975, Energetics of ligand binding to proteins, Adv. Protein Chem. 29: 1–83.PubMedCrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1985

Authors and Affiliations

  • W. D. Stein
    • 1
  1. 1.Department of Biological Chemistry, Institute of Life SciencesHebrew UniversityJerusalemIsrael

Personalised recommendations