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Can free energy transduction be localized at some crucial part of the enzymatic cycle?

Published online by Cambridge University Press:  17 March 2009

Terrell L. Hill  and
Evan Eisenberg
Terrell L. Hill
Affiliation:
Laboratory of Molecular Biology, National Institute of Arthritis, Metabolism and Digestive Diseases and Laboratory of Cell Biology, National Heart, Lung, and Blood Institute, National Instiutes of Health, Bethesda, Maryland, 20205
Evan Eisenberg
Affiliation:
Laboratory of Molecular Biology, National Institute of Arthritis, Metabolism and Digestive Diseases and Laboratory of Cell Biology, National Heart, Lung, and Blood Institute, National Instiutes of Health, Bethesda, Maryland, 20205
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Extract

Our concern here will be with energetic rather than kinetic aspects of how a macromolecular enzyme molecule or enzyme complex in a biological membrane accomplishes the transfer or transduction of one kind of small-molecule free energy into another. An example is the use of the free energy of ATP hydrolysis (to form ADP and P1) to move Ca2+ across a membrane against its own electrochemical potential gradient (Stryer, 1981). In this case, the free energy decreases in the hydrolysis reaction but much of this is recovered in the form of an increase in free energy of the Ca2+ ions (the remainder is dissipated as heat). There is, of course, no net change in the free energy of the enzyme itself (Ca-ATPase).

Type
Research Article
Information
Quarterly Reviews of Biophysics , Volume 14 , Issue 4 , November 1981 , pp. 463 - 511
Copyright
Copyright © Cambridge University Press 1981

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References

(X) REFERENCES

Albery, W. J. & Knowles, J. R. (1976). Free energy profile for the reaction catalysed by triosephosphate. Biochemistry, N.Y. 15, 5627–5640.Google Scholar
Alexandre, A., Reynafarje, B. & Lehninger, A. L. (1978). Stoichiometry of vectorial H+ movements coupled to electron transport and to ATP synthesis in mitochondria. Proc. natn. Acad. Sci. U.S.A. 75, 5296–5300.Google Scholar
Boyer, P. D. (1974). Conformational coupling in biological energy transductions. In Dynamics of Energy-Transducing Membranes (ed. Ernster, L., Estabrook, R. W. and Slater, E. C.), pp. 289–301. Amsterdam: Elsevier.Google Scholar
Boyer, P. D. (1977). Coupling mechanisms in capture, transmission, and use of energy. A. Rev. Biochem. 46, 957–966.Google Scholar
Caplan, S. R. (1981 a). Efficiency of energy transduction by bacteriorhodopsin: an approach using the Hill diagram method. In Dynamic Aspects of Biopolyelectrolytes and Biomembranes (ed. Oosawa, F., Imai, N., Miller, I. R., Sugai, S. and Kobatake, Y.), in the Press. Amsterdam: Elsevier.Google Scholar
Caplan, S. R. (1981 b). Reciprocity or near-reciprocity of highly-coupled enzymatic processes at the multidimensional inflection point. Proc. natn. Acad. Sci. U.S.A. (in the press).CrossRefGoogle Scholar
Chance, B. (1977). Electron transfer: pathways, mechanisms, and controls. A. Rev. Biochem. 46, 967–980.CrossRefGoogle ScholarPubMed
Eisenberg, E., Hill, T. L. & Chen, Y. (1980). Cross-bridge model of muscle contraction: quantitative analysis. Biophys. J. 29, 195–227.CrossRefGoogle ScholarPubMed
Gutfreund, H. & Trentham, D. R. (1975). Energy changes during the formation and interconversion of enzyme-substrate complexes. In Energy Transformation in Biological Systems, pp. 69–81. Ciba Fdn. Symp. no. 31. Amsterdam: Associated Scientific Publishers.Google Scholar
Hill, T. L. (1950). Statistical mechanics of adsorption. IX. Adsorption thermodynamics and solution thermodynamics. J. Chem. Phys. 18, 246–256.Google Scholar
Hill, T. L. (1960). Statistical Thermodynamics. Reading, Mass.: Addison–Wesley.Google Scholar
Hill, T. L. (1969). A proposed common allosteric mechanism for active transport, muscle contraction, and ribosomal translocation. Proc. natn. Acad. Sci. U.S.A. 64, 267–274.Google Scholar
Hill, T. L. (1977 a). Biochemical cycles and free energy transduction Trends Biochem. Sci. 2, 204–207.Google Scholar
Hill, T. L. (1977 b). Free Energy Transduction in Biology. New York: Academic.Google Scholar
Hill, T. L. (1979). Coupled enzyme systems in a vesicular membrane: oxidative phosphorylation as an example. Proc. natn. Acad. Sci. U.S.A. 76, 232–235.CrossRefGoogle Scholar
Hill, T. L. & Eisenberg, E. (1980). Theoretical considerations in the equilibrium binding of myosin fragments on F-actin. Biophys. Chem. 11, 271–281.Google Scholar
Jencks, W. P. (1980 a). The utilization of binding energy in coupled vectorial processes. Adv. Enzymol. 51, 75–106.Google ScholarPubMed
Jencks, W. P. (1980 b). What everyone wanted to know about tight binding and enzyme catalysis but never thought of asking. In Chemical Recognition in Biology (ed. Chapeville, F. and Haenni, A.), pp. 3–25. New York: Springer.Google Scholar
Kedem, O. & Caplan, S. R. (1965). Degree of coupling and its relation to efficiency of energy conversion. Trans. Faraday Soc. 61, 1897–1911.CrossRefGoogle Scholar
King, E. L. & Altman, C. (1956). A systematic method for deriving the rate laws for enzyme-catalysed reactions. J. Phys. Chem. 60, 1375–1378.CrossRefGoogle Scholar
Knowles, J. R. (1980). Enzyme-catalysed phosphoryl transfer reactions. A. Rev. Biochem. 49, 877–919.CrossRefGoogle Scholar
Koshland, D. E. (1958). Application of a theory of enzyme specificity to protein synthesis. Proc. natn. Acad. Sci. U.S.A. 44, 98–104.CrossRefGoogle ScholarPubMed
Koshland, D. E. & Neet, K. E. (1967). The catalytic and regulatory properties of enzymes. A. Rev. Biochem. 37, 359–410.CrossRefGoogle Scholar
Lehninger, A. L. (1975). Biochemistry. New York: Worth.Google Scholar
Mitchell, P. (1973 a). Chemiosmotic coupling in energy transduction: a logical development of biochemical knowledge. In Membrane Structure and Mechanisms of Biological Energy Transduction (ed. Avery, J.), pp. 5–24. London: Plenum.Google Scholar
Mitchell, P. (1973 b). Performance and conservation of osmotic work by proton-coupled solute porter systems. In Membrane Structure and Mechanism of Biological Energy Transduction (ed. Avery, J.), pp. 265–293.CrossRefGoogle Scholar
Robinson, J. D. & Flashner, M. S. (1979). The (Na++K+)-activated ATPase: enzymatic and transport properties. Biochim. biophys. Acta 549, 145–176.Google Scholar
Stryer, J. W. (1981). Biochemistry. San Francisco: Freeman.Google Scholar
Stucki, J. W. (1980). The optimal efficiency and economic degrees of coupling of oxidative phosphorylation. Eur. J. Biochem. 109, 269–283.Google Scholar
Tanford, C. (1981). Chemical potential of bound ligand, an important parameter for free energy transduction. Proc. natn. Acad. Sci. U.S.A. 78, 270–273.Google Scholar
Weber, G. (1975). Energetics of ligand binding to proteins. Adv. Protein Chem. 29, 1–83.CrossRefGoogle ScholarPubMed
Wyman, J. (1964). Linked functions and reciprocal effects in hemoglobin: a second look. Adv. Protein Chem. 19, 223–286.CrossRefGoogle ScholarPubMed