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Deuterium isotope effects on noncovalent interactions between molecules. Export

Chemico-biological interactions, Vol. 117, No. 3. (12 February 1999), pp. 191-217.

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d2o dtra heavywater isotopeffects ksie review

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I only read a few parts of this review, but I think it has some valuable parts, especially since Wade is trying to focus on reviewing isotope affects that are unlikely due to direct involvement of a deuterium bond in a chemical reaction. For example, effects on biomolecular interactions due to the differences in the solvent.

There is a very interesting section which reviews some prior work on deuteration and olfaction. It references some work with whitefish smelling deuterated glycine, and insects responding to deuterated molecules such as acetone. Also it references Turin's work.

skoch3 (public note) - 2009-11-04 23:48:12

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The topic of deuterium isotope effects is usually concerned with the effects on chemical reactions that are caused by the substitution of deuterium atoms for protium, or hydrogen, atoms in a molecule. These effects include changes in the rate of cleavage of covalent bonds to deuterium, or to an atom located adjacent to deuterium, in a reactant molecule. Deuterium isotope effects on other, noncovalent, interactions between molecules are known to occur, but they are generally considered to be insignificant, especially in biological experiments where deuterium substituted molecules are used as tracers. Noncovalent interactions between molecules include hydrogen bonding, and ionic and van der Waals interactions. This article reviews evidence for deuterium isotope effects on noncovalent interactions, with an emphasis on binding interactions between molecules of biological interest, but also including examples of nonbiological molecules in order to demonstrate the generality of these effects. The reality of this effect relies on the assumption that the only difference between the isotopomers considered is the presence of deuterium or hydrogen; there are no impurities present. The physical basis of the effect may be due to differences in the polarities and/or sizes of deuterated versus nondeuterated isomers, and the extent of a deuterium isotope effect on a noncovalent interaction depends on the site of deuteration within a biomolecule. The presence of this effect requires careful interpretation of results obtained in experiments with deuterium labeled compounds.


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