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Biological thermodynamics

From Wikipedia, the free encyclopedia

Biological thermodynamics is a phrase that is sometimes used to refer to bioenergetics, the study of energy transformation in the biological sciences. Biological thermodynamics may be defined as 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.


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 K. Burton, to contain equilibrium constants and Gibbs free energy of formations for chemical species, able to calculate biochemical reactions that had not yet occurred.[2]

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 they live in symbiosis with their environment. Energy transformations in biology are primarily dependent 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.[3] Annual energy captured by photosynthesis in green plants is about 4% of the total sunlight energy which reaches Earth. The energy transformations in biological communities surrounding hydrothermal vents are exceptions; they oxidize sulfur, obtaining their energy via chemosynthesisrather than photosynthesis. [edit]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,[4] and other such essential energy controlled pathways. Thermodynamically, 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. [edit]Examples [edit]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 neither be created nor destroyed.[5] 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.[6] [edit]Second

Law of Thermodynamics

The Second Law of Thermodynamics is primarily concerned 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.[7] 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, only must simply refer 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 clearly involves an increase of order. If the virus is

Therefore. energy and entropy generally change together. 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. Therefore.considered an isolated system. Likewise. this reaction will not occur spontaneously. In this case. this process would be in defiance of the Second Law.[8] [edit]Gibbs Free Energy In biological systems. it is necessary to be able to define a state function which accounts for these changes simultaneously. These two reactions can be coupled together. G = H − TS where:    H is the enthalpy (SI unit: joule) T is the temperature (SI unit: kelvin) S is the entropy (SI unit: joule per kelvin) The change in Gibbs Free Energy can be used to determine whether a given chemical reaction can occur spontaneously. if ∆G is positive. The breakdown of ATP to form ADP and inorganic phosphate has a ∆G value of -7. G. The ∆G value of the coupled reaction is -1. the reaction is nonspontaneous. the reaction of glucose with fructose to form sucrose has a ∆G value of +5. indicating that the reaction will occur spontaneously. a virus molecule interacts directly with its environment. If ∆G is negative.3 kcal/mole.5 kcal/mole. highly favorable reaction (negative ∆G2 where the magnitude of ∆G2 > magnitude of ∆G1). This state function is the Gibbs Free Energy. the overall Gibbs Free Energy change is simply the sum of the ∆G values for each reaction. This principle of coupling reactions to alter the change in Gibbs Free Energy is the basic principle behind all enzymatic action in biological organisms . an unfavorable reaction (positive ∆G1) can be driven by a second. Therefore. However. The glucose-1-phosphate is then able to bond with fructose yielding sucrose and inorganic phosphate. For example. so that glucose binds with ATP to form glucose-1-phosphate and ADP.[9] Chemical reactions can be “coupled” together if they share intermediates.8 kcal/mole. the reaction can occurspontaneously.