The receptor site for chloramphenicol in vitro and in vivo

  • Olaf Pongs
Part of the Biological Council book series (BCSDA)


Chloramphenicol inhibits protein synthesis in Gram-negative and Gram-positive bacteria as well as in chloroplasts, blue-green algae and mitochondria (for a review, see Pestka, 1971). It was the first antibiotic to be synthesised by chemical methods (Controulis, Rebstock and Crooks, 1949). The molecule has a relatively simple structure, which consists of a propanediol moiety (III), carrying a p-nitrobenzene side-chain (I) and a dichloroacetyl side-chain (II) (Fig. 10.1).


Ribosomal Protein Receptor Site Affinity Probe Peptidyltransferase Centre Affinity Labelling 
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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  1. Bald, R., Erdmann, V. A. and Pongs, O. (1972). FEBS Lett., 28, 149PubMedCrossRefGoogle Scholar
  2. Celma, M. L., Monro, R. and Vazquez, D. (1971). FEBS Lett., 13, 247PubMedCrossRefGoogle Scholar
  3. Controulis, M., Rebstock, M. C. and Crooks, H. M. (1949). J. Amer. Chem. Soc., 71, 2458CrossRefGoogle Scholar
  4. Czernilofsky, A. P., Collatz, E. E., Stöffler, G. and Kuchler, E. (1974). Proc. Nat. Acad. Sci. U.S.A., 71, 230CrossRefGoogle Scholar
  5. Das, H. K., Goldstein, A. and Kanner, L. C. (1966). Mol. Pharma col., 2, 158Google Scholar
  6. Fernandez-Munoz, R., Monro, R. E., Torres-Pinedo, R. and Vazquez, D. (1971). Eur. J. Biochem., 23, 185PubMedCrossRefGoogle Scholar
  7. Hahn, F. E. and Gund, P. (1975). Topics in Infectious Diseases (ed. J. Drews and F. E. Hahn), Springer, Vienna, p. 245Google Scholar
  8. Hahn, F. E., Hayes, J. E., Wisseman, C. L., Hopps, H. E. and Smadel, J. E. (1956). Antibiot. Chemother., 6, 531Google Scholar
  9. Hansch, C., Nakamoto, K., Gorin, M., Denisevich, P., Garrett, E. R. and Won, C. H. (1973). J. Med. Chem., 16, 917PubMedCrossRefGoogle Scholar
  10. Homann, H. E. and Nierhaus, K. H. (1971). Eur. J. Biochem., 20, 249PubMedCrossRefGoogle Scholar
  11. Kolosov, M. N., Shemiakin, M. M., Khokhlov, A. S. and Gurevich, A. I. (1961). Khimia Antibiotikov I, Iedatoto Akademii Nauk USSRGoogle Scholar
  12. Maxwell, R. E. and Nickel, V. S. (1954). Antibiot. Chemother., 4, 289Google Scholar
  13. Nathans, D. (1964). Proc. Nat. Acad. Sci. U.S.A., 51, 585CrossRefGoogle Scholar
  14. Nierhaus, D. and Nierhaus, K. H. (1973). Proc. Nat. Acad. Sci. USA, 70, 2224PubMedPubMedCentralCrossRefGoogle Scholar
  15. Oen, H., Pellegrini, M., Eilat, D. and Cantor, C. (1973). Proc. Nat. Acad. Sci. USA, 70, 2799PubMedPubMedCentralCrossRefGoogle Scholar
  16. Pellegrini, M. (1973). Ph.D. dissertation, Columbia University, New YorkGoogle Scholar
  17. Pestka, S. (1969). Proc. Nat. Acad. Sci. USA, 64, 709PubMedPubMedCentralCrossRefGoogle Scholar
  18. Pestka, S. (1971). Ann. Rev. Microbiol., 25, 487CrossRefGoogle Scholar
  19. Pongs, O., Bald, R. and Erdmann, V. A. (1973). Proc. Nat. Acad. Sci. USA, 70, 2229PubMedPubMedCentralCrossRefGoogle Scholar
  20. Pongs, 0., Bald, R., Erdmann, V. A. and Reinwald, E. (1975). Topics in Infectious Diseases (ed. J. Drews and F. E. Hahn), Springer, Vienna, p. 179Google Scholar
  21. Pongs, O., Nierhaus, K. H., Erdmann, V. A. and Wittmann, H. G. (1974). FEBS Lett., 40, S 28CrossRefGoogle Scholar
  22. Pongs, O. and Messer, W. (1976). J. Mol. Biol., 101, 171PubMedCrossRefGoogle Scholar
  23. Rebstock, M. C., Tratton, C. D. and Bambas, L. L. (1955). J. Amer. Chem. Soc., 77, 24CrossRefGoogle Scholar
  24. So, A. G. and Davie, E. W. (1963). Biochemistry, 2, 132PubMedCrossRefGoogle Scholar
  25. Sonenberg, N., Wilchek, M. and Zamir, A. (1973). Proc. Nat. Acad. Sci. USA, 70, 1423PubMedPubMedCentralCrossRefGoogle Scholar
  26. Stöffler, G. and Tischendorf, G. W. (1975). Topics in Infectious Diseases (ed. J. Drews and F. E. Hahn), Springer, Vienna, p. 117Google Scholar
  27. Tischendorf, G. W., Zeichhardt, H. and Stöffler, G. (1975). Proc. Nat. Acad. Sci. USA, 72, 4201CrossRefGoogle Scholar
  28. Vazquez, D. (1964). Biochim. Biophys.Acta, 114, 277CrossRefGoogle Scholar
  29. Vazquez, D. (1974). FEBS Lett., Suppl. 40, 63CrossRefGoogle Scholar
  30. Weber, H. J. (1972). Molec. Gen. Genet., 119, 233PubMedCrossRefGoogle Scholar
  31. Weber, M. J. and DeMoss, J. A. (1969). J. Bacteriol., 97, 1099PubMedPubMedCentralGoogle Scholar
  32. Wittmann, H. G. (1976). Eur. J. Biochem., 61, 1PubMedCrossRefGoogle Scholar

Copyright information

© Institute of Biology Endowment Trust Fund 1977

Authors and Affiliations

  • Olaf Pongs
    • 1
  1. 1.MRC Laboratory of Molecular BiologyCambridgeUK

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