The role of deuterium in molecular evolution

A principal feature of the structure of such biologically important compounds as proteins and nucleic acids is the maintenance of their structure by virtue of the participation of many hydrogen bonds in macromolecule. One may expect that the hydrogen bonds formed by of many deuterium will be different in their energy from those formed by proton. The differences in the nuclear mass of hydrogen and deuterium may possibly cause disturbances in the DNA-synthesis, leading to permanent changes in its structure and consequently in the cells genotype. The multiplication which would occur in macromolecules of even a small difference between a proton and a deuteron bond would certainly have the effect upon its structure.

The sensitivity of enzyme function to structure and the presumed sensitivity of nucleic acids function (genetic and mitotic) to its structure would lead one to expect a noticeable effect on the metabolic pattern and reproductive behavior of the organism. And next, the changes in dissociation constants of DNA and protein ionizable groups when transfer the macromolecule from water to ²H₂O may perturb the charge state of the DNA and protein. Substitution of ¹H for deuterium also affects the stability and geometry of hydrogen bonds in apparently rather complex way and may, through the changes in the hydrogen bond zero-point vibrational energies, alter the conformational dynamics of hydrogen (deuterium)-bonded structures within the DNA and protein in ²H₂O.

5. CONCLUSION

The successful adaptation of organisms to high concentration of ²H₂O will open a new avenues of investigation with using [U- ²H]labeled macromolecules could be isolated from these organisms. For example, fully deuterated essential macromolecules as proteins and nucleic acids will give promise of important biological, medical and diagnostical uses. Modern physical methods of study the structure of [U- ²H]labeled macromolecules, particularly three-dimentional NMR in a combination with crystallography methods, X-ray diffraction, IR-, and CD- spectroscopy should cast new light on many obscure problems concerning with the biological introduction of deuterium into molecules of DNA and proteins as well as the structure and the function of macromolecules in the presence of ²H₂O. The variety of these and other aspects of biophysical properties of fully deuterated macromolecules in the presence of ²H₂O remain an interesting task for the future.

First, I hope that the structural and the functional studies of [U- ²H]labeled macromolecules can provide us to the useful information about a many aspects of the synthesis of fully deuterated macromolecules and their biophysical behaviour in ²H₂O.

Second, the extensive body of available structural data about a cell protection system (at the level of the structure and the functioning of [U- ²H]labeled DNA and enzymes) will also form the basis for a particularly useful model for the study of biological adaptation to ²H₂O in aspect of molecular evolution of macromolecules with difined isotopic structures.

Finally, we also believe, the research can make a favour the medicine and biotechnology, especially for creating a fully deuterated analogues of enzymes and DNA having something different properties then the protonated species and working in the presence of ²H₂O.

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