Biological thermodynamics

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Biological thermodynamics is the quantitative study of the energy transductions that occur in and between living organisms, structures, and cells and of the nature and function of the chemical processes underlying these transductions. Biological thermodynamics may address the question of whether the benefit associated with any particular phenotypic trait is worth the energy investment it requires.

History

German-British medical doctor and biochemist Hans Krebs' 1957 book Energy Transformations in Living Matter (written with Hans Kornberg)[1] was the first major publication on the thermodynamics of biochemical reactions. In addition, the appendix contained the first-ever published thermodynamic tables, written by Kenneth Burton, to contain equilibrium constants and Gibbs free energy of formations for chemical species, able to calculate biochemical reactions that had not yet occurred.

Non-equilibrium thermodynamics has been applied for explaining how biological organisms can develop from disorder. Ilya Prigogine developed methods for the thermodynamic treatment of such systems. He called these systems dissipative systems, because they are formed and maintained by the dissipative processes that exchange energy between the system and its environment, and because they disappear if that exchange ceases. It may be said that they live in symbiosis with their environment. Energy transformations in biology are dependent primarily on photosynthesis. The total energy captured by photosynthesis in green plants from the solar radiation is about 2 x 1023 joules of energy per year.[2] Annual energy captured by photosynthesis in green plants is about 4% of the total sunlight energy that reaches Earth. The energy transformations in biological communities surrounding hydrothermal vents are exceptions; they oxidize sulfur, obtaining their energy via chemosynthesis rather than photosynthesis.

The focus of thermodynamics in biology

The field of biological thermodynamics is focused on principles of chemical thermodynamics in biology and biochemistry. Principles covered include the first law of thermodynamics, the second law of thermodynamics, Gibbs free energy, statistical thermodynamics, reaction kinetics, and on hypotheses of the origin of life. Presently, biological thermodynamics concerns itself with the study of internal biochemical dynamics as: ATP hydrolysis, protein stability, DNA binding, membrane diffusion, enzyme kinetics,[3] and other such essential energy controlled pathways. In terms of thermodynamics, the amount of energy capable of doing work during a chemical reaction is measured quantitatively by the change in the Gibbs free energy. The physical biologist Alfred Lotka attempted to unify the change in the Gibbs free energy with evolutionary theory.

Examples

First Law of Thermodynamics

The First Law of Thermodynamics is a statement of the conservation of energy; though it can be changed from one form to another, energy can be neither created nor destroyed.[4] From the first law, a principle called Hess's Law arises. Hess’s Law states that the heat absorbed or evolved in a given reaction must always be constant and independent of the manner in which the reaction takes place. Although some intermediate reactions may be endothermic and others may be exothermic, the total heat exchange is equal to the heat exchange had the process occurred directly. This principle is the basis for the calorimeter, a device used to determine the amount of heat in a chemical reaction. Since all incoming energy enters the body as food and is ultimately oxidized, the total heat production may be estimated by measuring the heat produced by the oxidation of food in a calorimeter. This heat is expressed in kilocalories, which are the common unit of food energy found on nutrition labels.[5]

Second Law of Thermodynamics

The Second Law of Thermodynamics is concerned primarily with whether or not a given process is possible. The Second Law states that no natural process can occur unless it is accompanied by an increase in the entropy of the universe.[6] Stated differently, an isolated system will always tend to disorder. Living organisms are often mistakenly believed to defy the Second Law because they are able to increase their level of organization. To correct this misinterpretation, one must refer simply to the definition of systems and boundaries. A living organism is an open system, able to exchange both matter and energy with its environment. Take, for example, the assembly of a virus molecule from its subunits, which involves an increase of order. If the virus is considered an isolated system, this process would be in defiance of the Second Law. However, a virus molecule interacts directly with its environment. The assembly of a virus molecule results in an increase of entropy in the system as a whole due to the liberation of water of solvation from the components and the resulting increase in rotational and translational entropy of the solvent.[7]

Gibbs Free Energy

In biological systems, in general energy and entropy change together. Therefore, it is necessary to be able to define a state function that accounts for these changes simultaneously. This state function is the Gibbs Free Energy, G.

G = H − TS

where:

The change in Gibbs Free Energy can be used to determine whether a given chemical reaction can occur spontaneously. If ∆G is negative, the reaction can occur spontaneously. Likewise, if ∆G is positive, the reaction is nonspontaneous.[8] Chemical reactions can be “coupled” together if they share intermediates. In this case, the overall Gibbs Free Energy change is simply the sum of the ∆G values for each reaction. Therefore, an unfavorable reaction (positive ∆G1) can be driven by a second, highly favorable reaction (negative ∆G2 where the magnitude of ∆G2 > magnitude of ∆G1). For example, the reaction of glucose with fructose to form sucrose has a ∆G value of +5.5 kcal/mole. Therefore, this reaction will not occur spontaneously. The breakdown of ATP to form ADP and inorganic phosphate has a ∆G value of -7.3 kcal/mole. These two reactions can be coupled together, so that glucose binds with ATP to form glucose-1-phosphate and ADP. The glucose-1-phosphate is then able to bond with fructose yielding sucrose and inorganic phosphate. The ∆G value of the coupled reaction is -1.8 kcal/mole, indicating that the reaction will occur spontaneously. This principle of coupling reactions to alter the change in Gibbs Free Energy is the basic principle behind all enzymatic action in biological organisms.[9]

See also

References

  1. ↑ Alberty R (2004). "A short history of the thermodynamics of enzyme-catalyzed reactions". J Biol Chem 279 (27): 27831–6. doi:10.1074/jbc.X400003200. PMID 15073189. 
  2. ↑ Akihiko Ito and Takehisa Oikawa. "Global Mapping of Terrestrial Primary Productivity and Light-Use Efficiency with a Process-Based Model". In M. Shiyomi et al. Global Environmental Change in the Ocean and on Land. pp. 343–358. 
  3. ↑ M.J. Farabee. "Reactions and Enzymes". On-Line Biology Book. Estrella Mountain Community College. 
  4. ↑ Haynie, Donald T. (2001). Biological Thermodynamics. Cambridge UP. ISBN 9780521795494. 
  5. ↑ Stacy, Ralph W., David T. Williams, Ralph E. Worden, and Rex O. McMorris. Essentials of Biological and Medical Physics. New York: McGraw-Hill Book, 1955. Print.
  6. ↑ Haynie, Donald T. Biological Thermodynamics. Cambridge: Cambridge UP, 2001. Print.
  7. ↑ Edsall, John T., and H. Gutfreund. Biothermodynamics: The Study of Biochemical Processes at Equilibrium. Chichester, West Sussex: Wiley, 1983. Print.
  8. ↑ Bergethon, P. R. The Physical Basis of Biochemistry: The Foundations of Molecular Biophysics. New York: Springer, 1998. Print.
  9. ↑ Alberts, Bruce. Essential Cell Biology. New York: Garland Science, 2009. Print.

Further reading

  • Haynie, D. (2001). Biological Thermodynamics (textbook). Cambridge: Cambridge University Press.
  • Lehninger, A., Nelson, D., & Cox, M. (1993). Principles of Biochemistry, 2nd Ed (textbook). New York: Worth Publishers.
  • Alberty, Robert, A. (2006). Biochemical Thermodynamics: Applications of Mathematica (Methods of Biochemical Analysis), Wiley-Interscience.

External links

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