Skip to main content Accessibility help

We use cookies to distinguish you from other users and to provide you with a better experience on our websites. Close this message to accept cookies or find out how to manage your cookie settings.

Close cookie message
×
Hostname: page-component-cd9895bd7-dzt6s Total loading time: 0 Render date: 2025-01-05T14:45:45.805Z Has data issue: false hasContentIssue false

Chapter 4 - Gibbs free energy – theory

Published online by Cambridge University Press:  05 June 2012

Donald T. Haynie
Donald T. Haynie
Affiliation:
Central Michigan University
Get access

Summary

Introduction

This chapter discusses a thermodynamic relationship that provides a basis for explaining spontaneous chemical reactivity, chemical equilibrium, and the phase behavior of chemical compounds. The relationship involves a thermodynamic state function that enables prediction of the direction of a chemical reaction at constant temperature and pressure. The constraints of fixed T and p might seem annoyingly restrictive, because they are less general than the requirements of the Second Law, but in fact the gains made on imposing the constraints will outweigh the losses. How is that? One reason is at any given time an individual organism is practically at uniform pressure and temperature (but be sure to see the Exercises at the end of the chapter). Another is that constant temperature and pressure are the very conditions under which nearly all bench-top biochemistry experiments are done. Yet another is that, although the total entropy of the universe must increase in order for a process to be spontaneous, evaluation of the total entropy change requires measurement of both the entropy change of the system and the entropy change of the surroundings. Whereas ΔSsystem can often be found without too much difficulty, albeit only indirectly, ΔSsurroundings can be hard to measure! How could one measure the entropy change of the rest of the universe? The subject of the present chapter provides a way around the difficulty.

Type
Chapter
Information
Biological Thermodynamics , pp. 85 - 133
Publisher: Cambridge University Press
Print publication year: 2008

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Arrhenius, S. (1912). Theories of Solution. New Haven: Yale University Press.Google Scholar
Atkins, P. W. (1994). The Second Law: Energy, Chaos, and Form, p. 167. New York: Scientific American.Google Scholar
Atkins, P. W. (1998). Physical Chemistry, 6th edn, cc. 10.2 & 23.2. Oxford: Oxford University Press.Google Scholar
Bada, J. L. & Miller, S. L. (1968). Equilibrium constant for the reversible deamination of aspartic acid. Biochemistry, 7, 3403–8.CrossRefGoogle ScholarPubMed
Banks, B. E. C. & Vernon, C. A. (1978). Biochemical abuse of standard equilibrium constants. Trends in Biochemical Sciences, 3, N156–8.Google Scholar
Bates, R. G. (1973). Determination of pH; Theory and Practice. New York: John Wiley.Google Scholar
Ben-Shem, A., Frolow, F. & Nelson, N. (2003). Crystal structure of plant photosystem I. Nature, 426, 630–5.CrossRefGoogle ScholarPubMed
Bergethon, P. R. (1998). The Physical Basis of Biochemistry: the Foundations of Molecular Biophysics, cc. 2.17, 13 & 21.4–21.6. New York: Springer-Verlag.CrossRefGoogle Scholar
Blandamer, M. J. (1992). Chemical Equilibrium in Solution. Hemel Hempstead: Ellis Horwood/Prentice-Hall.Google Scholar
Bradley, J. (1990). Teaching electrochemistry. Education in Chemistry, 27, 48–50.Google Scholar
Bretscher, M. S. (1985). The molecules of the cell membrane. Scientific American, 253, no. 4, 86–90.CrossRefGoogle ScholarPubMed
Butcher, J. (2005). Profile: Lewis Gordon Pugh – polar swimmer. The Lancet, 366, S23–4.CrossRefGoogle Scholar
Christensen, H. N. & Cellarius, R A. (1972). Introduction to Bioenergetics: Thermodynamics for the Biologist: A Learning Program for Students of the Biological and Medical Sciences. Philadelphia: W. B. Saunders.Google Scholar
Creighton, T. E. (1993). Proteins: Structures and Molecular Properties, 2nd edn, ch. 7. New York: W. H. Freeman.Google Scholar
Dawes, E. A. (1962). Quantitative Problems in Biochemistry, 2nd edn, ch. 1. Edinburgh: E. & S. Livingstone.Google Scholar
Dawson, R. M. C., Elliott, D. C., Elliott, W. H. & Jones, K. M. (1986). Data for Biochemical Research, 3rd edn. Oxford: Clarendon Press.Google Scholar
DeKock, R. L. (1996). Tendency of reaction, electrochemistry, and units. Journal of Chemical Education, 73, 955–6.CrossRefGoogle Scholar
DeVries, A. L. (1982). Biological antifreeze agents in coldwater. Comparative Biochemistry and Physiology, 73A, 627–40.CrossRefGoogle Scholar
Ellis, R. J. (2001). Macromolecular crowding: Obvious but underappreciated. Trends in Biochemical Sciences, 26, 597–604.CrossRefGoogle ScholarPubMed
Encyclopædia Britannica CD98, “Activity Coefficient,” “Arrhenius Theory,” “Boiling Point,” “Debye–Hückel Equation,” “Equilibrium,” “Free Energy,” “Freezing Point,” “Ideal Solution,” “Life,” “Melting Point,” and “Phase.”
Feeney, R. E. (1974). A biological antifreeze. American Scientist, 62, 712–19.Google ScholarPubMed
Feiner, A. S. & McEvoy, A. J. (1994). The Nernst equation. Journal of Chemical Education, 71, 493–4.CrossRefGoogle Scholar
Franzen, H. F. (1988). The freezing point depression law in physical chemistry: is it time for a change?Journal of Chemical Education, 65, 1077–8.CrossRefGoogle Scholar
Fruton, J. S. (1999). Proteins, Enzymes, Genes: the Interplay of Chemistry and Biology. New Haven: Yale University Press.Google Scholar
Gennix, R. B. (1989). Biomembranes: Molecular Structure and Function. New York: Springer-Verlag.CrossRefGoogle Scholar
German, B. & Wyman, J. (1937). The titration curves of oxygenated and reduced hemoglobin. Journal of Biological Chemistry, 117, 533–50.Google Scholar
Gillispie, Charles C. (ed.) (1970). Dictionary of Scientific Biography. New York: Charles Scribner.Google Scholar
Good, N. E., Winter, W., Connolly, T. N., Izawa, S. & Singh, R. M. M. (1966). Hydrogen ion buffers for biological research. Biochemistry, 5, 467–76.CrossRefGoogle ScholarPubMed
Green, R. L. & Warren, G. J. (1985). Physical and functional repetition in a bacterial ice nucleation gene. Nature, 317, 645–8.CrossRefGoogle Scholar
Gurney, R. W. (1953). Ionic Processes in Solution. New York: McGraw-Hill.Google Scholar
Harned, H. S. & Owen, B. B. (1958). The Physical Chemistry of Electrolytic Solutions. Princeton: Van Nostrand-Reinhold.Google Scholar
Harold, F. M. (1986). The Vital Force: a Study of Bioenergetics, cc. 1 & 2. New York: W. H. Freeman.Google Scholar
Harris, D. A. (1995). Bioenergetics at a Glance, ch. 1. Oxford: Blackwell Science.Google Scholar
Haynie, D. T. (1993). The Structural Thermodynamics of Protein Folding, ch. 4. Ph.D. thesis, The Johns Hopkins University.Google Scholar
Hodgman, C. D. (ed.) (1957). C.R.C. Standard Mathematical Tables, 11th edn. Cleveland, Ohio: Chemical Rubber Company.Google Scholar
Hopkin, M. (2005). Man breaks world records with Antarctic swim. Nature News, 20 December.Google Scholar
Howlett, G. J., Blackburn, M. N., Compton, J. G. & Schachman, H. K. (1977). Allosteric regulation of aspartate transcarbamoylase. Analysis of the structural and functional behavior in terms of a two-state model. Biochemistry, 126, 5091–9.CrossRefGoogle Scholar
Hubbard, R. (1966). The stereoisomerization of 11-cis-retinal. Journal of Biological Chemistry, 241, 1814–18.Google ScholarPubMed
Kemp, H. R. (1987). The effect of temperature and pressure on equilibria: a derivation of the van't Hoff rules. Journal of Chemical Education, 64, 482–4.CrossRefGoogle Scholar
Klotz, I. M. (1986). Introduction to Biomolecular Energetics, cc. 3–7. Orlando: Academic Press.Google Scholar
Kondepudi, D. & Prigogine, I. (1998). Modern Thermodynamics: from Heat Engines to Dissipative Structures, cc. 7.5, 8.2 & 8.3. Chichester: John Wiley.Google Scholar
Koryta, J. (1992). Ions, Electrodes, and Membranes. New York: John Wiley.Google Scholar
Lodish, H., Baltimore, D., Berk, A., Zipursky, S. L., Matsudaira, P. & Darnell, J. (1995). Molecular Cell Biology, 3rd edn, ch. 2. New York: W. H. Freeman.Google Scholar
Marshall, C. B., Fletcher, G. L. & Davies, P. L. (2004) Hyperactive antifreeze protein in a fish, Nature, 429, 153.CrossRefGoogle ScholarPubMed
McPartland, A. A. & Segal, I. H. (1986). Equilibrium constants, free energy changes and coupled reactions: concepts and misconceptions. Biochemical Education, 14, 137–41.CrossRefGoogle Scholar
Millar, D., Millar, I., Millar, J. & Millar, M. (1989). Chambers Concise Dictionary of Scientists. Cambridge: Chambers.Google Scholar
Nicholls, D. G. & Ferguson, S. J. (1992). Bioenergetics 2. London: Academic Press.Google Scholar
Ochs, R. S. (1996). Thermodynamics and spontaneity. Journal of Chemical Education, 73, 952–4.CrossRefGoogle Scholar
Ostro, M. J. (1987). Liposomes. Scientific American, 256(1), 102–11.CrossRefGoogle ScholarPubMed
Palmer, C. M., Siebke, K. & Yeates, D. K. (2004). Infrared video thermography: a technique for assessing cold adaptation in insects. BioTechniques, 37, 212–17.Google ScholarPubMed
Peusner, L. (1974). Concepts in Bioenergetics, cc. 3, 5, 6 & 7. Englewood Cliffs: Prentice-Hall.Google Scholar
Price, G. (1998). Thermodynamics of Chemical Processes, ch. 4. Oxford: Oxford University Press.Google Scholar
Schrake, A., Ginsburg, A. & Schachman, H. K. (1981). Calorimetric estimate of the enthalpy change for the substrate-promoted conformational transition of aspartate transcarbamoylase from Escherichia coli. Journal of Biological Chemistry, 256, 5005–15.Google Scholar
Schultz, S. G. (1980). Basic Principles of Membrane Transport. Cambridge: Cambridge University Press.Google Scholar
Segal, I. H. (1976). Biochemical Calculations: How to Solve Mathematical Problems in General Biochemistry, 2nd edn, ch. 3. New York: John Wiley.Google Scholar
Smith, C. A. & Wood, E. J. (1991). Energy in Biological Systems, cc. 1.3 & 1.4. London: Chapman & Hall.CrossRefGoogle Scholar
Snell, F. M., Shulman, S., Spencer, R. P. & Moos, C. (1965). Biophysical Principles of Structure and Function. Reading, Massachusetts: Addison-Wesley.Google Scholar
Spencer, J. N. (1992). Competitive and coupled reactions, Journal of Chemical Education, 69, 281–4.CrossRefGoogle Scholar
Tanford, C. & Hauenstein, J. D. (1956). Hydrogen ion equilibria of ribonuclease. Journal of the American Chemical Society, 78, 5287–91.CrossRefGoogle Scholar
Tombs, M. P. & Peacocke, A. R. (1974). The Osmotic Pressure of Biological Macromolecules. Oxford: Clarendon Press.Google Scholar
Tydoki, R. J. (1995). Spontaneity, accessibility, irreversibility, ‘useful work’: the availability function, the Helmholtz function and the Gibbs function, Journal of Chemical Education, 72, 103–12.Google Scholar
Tydoki, R. J. (1996). The Gibbs function, spontaneity, and walls. Journal of Chemical Education, 73, 398–403.Google Scholar
Holde, K. E. (1985). Physical Biochemistry, 2nd edn, cc. 2.1, 2.3, 2.4 & 3. Englewood Cliffs: Prentice-Hall.Google Scholar
Voet, D. & Voet, J. G. (1995). Biochemistry, 2nd edn, cc. 2–2, 3, 4, 11–2, 15–4–15–6, 16, 18–1, 19–1, 28–3 & 34–4B. New York: Wiley.Google Scholar
Williams, T. I. (ed.) (1969). A Biographical Dictionary of Scientists. London: Adam & Charles Black.Google Scholar
Wood, S. E. & Battino, R. (1996). The Gibbs function controversy. Journal of Chemical Education, 73, 408–11.Google Scholar
Wrigglesworth, J. (1997). Energy and Life, cc3, 5.7.2, 7.1, 7.3 & 7.5.1. London: Taylor & Francis.CrossRefGoogle Scholar

Save book to Kindle

To save this book to your Kindle, first ensure [email protected] is added to your Approved Personal Document E-mail List under your Personal Document Settings on the Manage Your Content and Devices page of your Amazon account. Then enter the ‘name’ part of your Kindle email address below. Find out more about saving to your Kindle.

Note you can select to save to either the @free.kindle.com or @kindle.com variations. ‘@free.kindle.com’ emails are free but can only be saved to your device when it is connected to wi-fi. ‘@kindle.com’ emails can be delivered even when you are not connected to wi-fi, but note that service fees apply.

Find out more about the Kindle Personal Document Service.

Available formats
×

Save book to Dropbox

To save content items to your account, please confirm that you agree to abide by our usage policies. If this is the first time you use this feature, you will be asked to authorise Cambridge Core to connect with your account. Find out more about saving content to Dropbox.

Available formats
×

Save book to Google Drive

To save content items to your account, please confirm that you agree to abide by our usage policies. If this is the first time you use this feature, you will be asked to authorise Cambridge Core to connect with your account. Find out more about saving content to Google Drive.

Available formats
×