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Origins of life

, Volume 5, Issue 1–2, pp 263–283 | Cite as

Experimental attempts for the study of the origin of optical activity on earth

  • W. Thiemann
  • W. Darge
Part IV/Precellular Organization

Abstract

Optical activity of natural compounds is a characteristic of our living world which is based on the asymmetry of the molecular set-up. It is hard to realize a biological cell which would be constructed from racemic compounds alone. Yet it seems attractive to ask why nature preferred onlyone of two possible enantiomers, e.g. the L-amino-acids and D-sugars. Was there or is there a chance for an antipodic biosphere constructed on the basis of the ‘unnatural’ enantiomers like D-amino-acids and L-sugars on Earth or elsewhere?-The paper presents in its first part a review about hypotheses that would be able to explain the apparent discrepancy between the expectation from laboratory experience and the observation that biological matter consists of extremely asymmetric molecules. The speculations found in literature are divided mainly into two categories: The first one interprets the appearance of optical activity by a chance process and its amplification by suitable means, the second one postulates a cogency leading to the chirality of the biosphere observed today. The discovery of the non-conservation of parity in nuclear physics stimulated a search for related ‘asymmetry effects’ in chemistry. Experiments were undertaken by some workers to construct possible laboratory models for the evolution of optical activity, but many of them failed due to different causes. On the other hand a number of papers has been published that were not directed specifically to the problem discussed, but could be interpreted on the basis of the various hypotheses. It is particularly interesting in this context to look into papers describing the crystallisation of racemates from solutions, that were published as early as 70 yr ago. —In its second part the paper deals with the study of the polymerization of racemic amino-acids as a model that would possibly allow a decision between the hypotheses for the origin of optical activity, — mere chance or a physical driving force determining the chirality of evolution. Since great care was taken to eliminate all sources of systematical errors, one expected-form the classical standpoint-racemic poly-peptides of absolute zero optical activity. — The monomer amino-acids (α-alanine, α-amino-butyric acid, and lysine) were racemized before the polymerization in order to guarantee ‘ideally racemic’ substrates. Polymerization was achieved via the N-carboxyanhydrides of the amino-acids. Reaction vessels and measuring cells were thoroughly cleaned with boiling chromic sulfuric acid and kept sealed from the laboratory atmosphere to prevent any contamination. The optical activity was determined in a Cary 60 spectropolarimeter calibrated to detect angles of rotations in the range of 0.5 mdeg with a maximum error of ±50%. All the poly-amino-acids investigated showed negative angles of rotation at 310 nm between 0.25 and 0.84 mdeg that would correspond to an hypothetical asymmetry effect-i.e. the relative difference of the polymerization constants of L-and D-amino-acids-in the order of 8×10−6. We believe that this result emphasises the existence of a physical force that enables a slight accumulation of the L-amino-acids within the high molecular weight polymers in excess to the D-amino-acids and could be of significance for the evolution of the biomass. At this point the experiments do not allow any conclusion about the nature of the observed ‘asymmetry effect’.

Keywords

Optical Activity Racemate Molecular Weight Polymer High Molecular Weight Polymer Living World 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. Applequist, J. and Doty, P.: 1962, inPolyaminoacids, Polypeptides and Proteins, Univ. Wisc. Press, Madison, p. 165.Google Scholar
  2. Bamford, C. H., Brown, L., Elliott, A., Hanby, W. E., and Trotter, I. F.: 1954,Nature 173, 27.Google Scholar
  3. Blout, E. R. and Idelson, M.: 1956,J. Am. Chem. Soc. 78, 3857.Google Scholar
  4. Byk, A.: 1904,Z. Phys. Chemie 49, 641.Google Scholar
  5. Campbell, A. N. and Garrow, F. C.: 1930,Trans. Farad. Soc. 26, 560.Google Scholar
  6. Copaux, H.: 1906,Ann. Chim. Phys. (8)7, 129.Google Scholar
  7. Copaux, H.: 1909a,Ann. Chim. Phys. (8)17, 234.Google Scholar
  8. Copaux, H.: 1909b,Compt. Rend. Acad. Sci. 143, 633.Google Scholar
  9. Copaux, H.: 1910a,Compt. Rend. Acad. Sci. 150, 475.Google Scholar
  10. Copaux, H.: 1910b,Bull. Soc. Min. 33, 167.Google Scholar
  11. Copaux, H.: 1912,Z. Kryst. 50, 317.Google Scholar
  12. Darmois, E.: 1952,Compt. Rend. Acad. Sci. 237, 124.Google Scholar
  13. Decker, P.: 1972,Z. Naturf. 27b, 257.Google Scholar
  14. Dongorozi, C. S.: 1969,Rev. Roum. Biochim. 6, 297.Google Scholar
  15. Fox, S. W., Harada, K., Krampitz, G., and Mueller, G.: 1970,Chem. Eng. Ind. News 48, 80.Google Scholar
  16. Garay, A. S.: 1968,Nature 219, 338.Google Scholar
  17. Harada, K.: 1970,Naturwiss 57, 114.Google Scholar
  18. Havinga, E.: 1954,Biochim. Biophys. Acta 13, 171.Google Scholar
  19. Hayatsu, R.: 1965,Science 149, 443.Google Scholar
  20. Kipping, F. S. and Pope, W. J.: 1903,J. Chem. Soc. 95, 103.Google Scholar
  21. Kortüm, G.: 1931,Ber. dtsch. Chem. Ges. 64, 1506.Google Scholar
  22. Kuhn, W. and Braun, E.: 1929,Naturwiss. 17, 227.Google Scholar
  23. Kuhn, W. and Knopf, E.: 1930,Naturwiss. 18, 183.Google Scholar
  24. Lee, T. D. and Yang, C. N.: 1956,Phys. Rev. 104, 254.Google Scholar
  25. Leuchs, H.: 1906,Ber. dtsch. Chem. Ges. 39, 857.Google Scholar
  26. Leuchs, H. and Manasse, W.: 1907,Ber dtsch. Chem. Ges. 40, 3235.Google Scholar
  27. Leuchs, H. and Geiger, W.: 1908,Ber. dtsch. Chem. Ges. 41, 1721.Google Scholar
  28. Mark, H. and Dostal, H.: 1935,Z. Phys. Chem. B 29, 299.Google Scholar
  29. Miller, S. L.: 1955,J. Am. Chem. Soc. 77, 2351.Google Scholar
  30. Moradpur, A., Nicoud, J. F., Balavoine, G., Kagan, H., and Tsoucaris, G.: 1971,J. Am. Chem. Soc. 93, 2353.Google Scholar
  31. Morowitz, H.: 1969,J. Theor. Biol. 25, 491.Google Scholar
  32. Mörtberg, L.: 1971,Nature 232, 105.Google Scholar
  33. Neuberger, A. N. and Sanger, F.: 1943,Biochem. J. 37, 515.Google Scholar
  34. Ogawa, T.: 1960, U. S. Patent2, 940, 998.Google Scholar
  35. Oparin, A.: 1971,Ideen exakt. Wiss. 1, 57.Google Scholar
  36. Ponnamperuma, C.: 1965,Science 1, 39.Google Scholar
  37. Seelig, F. F.: 1971,J. Theor. Biol. 31, 355.Google Scholar
  38. Shalitin, Y. and Katchalski, E.: 1960,J. Am. Chem. Soc. 82, 1630.Google Scholar
  39. Stahmann, M. A. (ed.): 1962,Polyaminoacids, Polypeptides, Proteins, Univ. Wisc. Press, Madison, p. 8.Google Scholar
  40. Thiemann, W. and Wagener, K.: 1970,Angew. Chem. (Int. ed.)9, 740.Google Scholar
  41. Ulbricht, T. L. V. and Vester, F.: 1962,Tetrahedron 18, 629.Google Scholar
  42. van't Hoff, J. H. and Dawson, T. M.: 1898,Ber. dtsch. Chem. Ges. 31, 528.Google Scholar
  43. Vester, F.: 1957, Seminar at Yale University, Feb. 7, 1957.Google Scholar
  44. Vogler, K. and Kofler, M.: 1956,Helv. Chim. Acta 39, 1387.Google Scholar
  45. Wada, A.: 1961,J. Mol. Biol. 3, 507.Google Scholar
  46. Wagener, K.: 1971, Private Communication.Google Scholar
  47. Wald, G.: 1957,Ann. N. Y. Acad. Sci. 69, 352.Google Scholar
  48. Wu, C. S., Ambler, E., Hayward, R. W., Hoppes, D. D., and Hudson, R. P.: 1957,Phys. Rev. 105, 1413.Google Scholar
  49. Wyrouboff, G.: 1896,Bull. Soc. Min. 19, 219.Google Scholar
  50. Yamagata, Y.: 1966,J. Theor. Biol. 11, 495.Google Scholar

Copyright information

© D. Reidel Publishing Company 1974

Authors and Affiliations

  • W. Thiemann
    • 1
  • W. Darge
    • 1
  1. 1.KernforschungsanlageInstitut für Physik. ChemieJülichF. R. G.

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