Transient Resonance Raman Spectra of Bacteriorhodopsin and Halorhodopsin

  • T. Ogura
  • A. Maeda
  • M. Nakagawa
  • T. Kitagawa
Part of the Springer Proceedings in Physics book series (SPPHY, volume 20)


Bacteriorhodopsin (bR) and halorhodopsin (hR) are light-dependent electrogenic proteins in the membrane of Halobacterium halobium (see Ref. 1 for a review). For both proteins, the species which have all-trans retinal chromophore linked to ε-nitrogen of lysine through a protonated Schiff base undergo the cis-trans isomerization to the 13-cis form upon illumination with light. The photo-isomerization of the chromophore is followed by a structural change of a protein moiety to compensate for the energy increase due to the charge separation between the protonated Schiff base and its counter anion. In the mechanism of the structural change a difference appears between the two proteins: unidirectional proton and chloride translocation through the membrane for bR and hR, respectively. In the case of bR, the Schiff base proton is transferred to the protein moiety upon the change from the L to M intermediates, which occurs on a µs time scale, but the photoreaction of hR is not accompanied by deprotonation of the Schiff base. It is interesting to study the structural details of the transient species of these two proteins on a µs time scale.


Schiff Base Probe Beam Pump Beam Difference Spectrum Raman Line 
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. 1.
    W. Stoeckenius, R. A. Bogomolni: Annu. Rev. Biochem. 52 587 (1982).CrossRefGoogle Scholar
  2. 2.
    L. Rimai, R. G. Kilponen, D. Gill: Biochem. Biophys. Res. Commun. 41 492 (1970).CrossRefGoogle Scholar
  3. 3.
    A. Lewis, J. Spoonhower, R. A. Bogomolni, R. H. Lozier, W. Stoeckenius: Proc. Natl. Acad. Sci. U.S.A. 71, 4462 (1974).ADSCrossRefGoogle Scholar
  4. 4.
    S. O. Smith, A. B. Meyers, R. A. Mathies, J. A. Pardoen, C. Winkel, E. M. M. van der Berg, J. Lugtenburg: Biophys. J. 47, 653 (1985).CrossRefGoogle Scholar
  5. 5.
    R. A. Mathies: In Spectroscopy of Biological Molecules (C. Sandorfy, T. Theophanides, eds.) p. 303 (1984).Google Scholar
  6. 6.
    M. E. Heyde, D. Gill, R. G. Kilponen, L. Rimai: J. Am. Chem. Soc. 93 6776 (1971).CrossRefGoogle Scholar
  7. 7.
    B. Aton, A. Doukas, R. H. Callender, B. Becher, T. G. Ebrey: Biochemistry 16 2955 (1977).CrossRefGoogle Scholar
  8. 8.
    T. Sugihara, T. Kitagawa: Bull. Chem. Soc. Jpn. 59 2929 (1986).CrossRefGoogle Scholar
  9. 9.
    M. Stockburger, T. Alshuth, D. Oesterhelt, W. Gartner: in Spectroscopy of Biological Systems (R. J. H. Clark, R. E. Hester, eds.) Wiley & Sons, p. 483 (1986).Google Scholar
  10. 10.
    A. Maeda, T. Ogura, T. Kitagawa: Biochemistry 25 2798 (1986).CrossRefGoogle Scholar
  11. 11.
    A. Maeda, T. Ogurusu, T. Yoshizawa, T. Kitagawa: Biochemistry 24, 2517 (1985).CrossRefGoogle Scholar
  12. 12.
    D. Oesterhelt, W. Stoeckenius: Methods Enzymol 31A 667 (1974).CrossRefGoogle Scholar
  13. 13.
    G. Wagner, D. Oesterhelt, G. Krippahl, J. K. Layni: FEBS Lett. 131 341 (1981).CrossRefGoogle Scholar
  14. 14.
    T. Ogurusu, A. Maeda, T. Yoshizawa: J. Biochem. 95 1073 (1984).Google Scholar
  15. 15.
    S.O. Smith, J. A. Pardoen, P. P. J. Mulder, B. Curry, J. Lugtenburg, R. A. Mathies: Biochemistry 22, 6141 (1983).CrossRefGoogle Scholar
  16. 16.
    J. Terner, C.-L. Hsieh, M. A. El-Sayed: Biophys. J. 26, 527 (1979).CrossRefGoogle Scholar
  17. 17.
    S. O. Smith, A. B. Myers, J. A. Pardoen, C. Winkel, P. P. J. Mulder, J. Lugtenburg, R. Mathies: Proc. Natl. Acad. Sci. U.S.A. 81 2055 (1984).ADSCrossRefGoogle Scholar
  18. 18.
    T. Alshuth, M. Stockburger: Photochem. Photobiol. 43 55 (1986).CrossRefGoogle Scholar
  19. 19.
    P. V. Argade, K. J. Rothschild: Biochemistry 22, 3460 (1983).CrossRefGoogle Scholar
  20. 20.
    A. Maeda: this book.Google Scholar
  21. 21.
    A. Lewis, M. A. Marcus, B. Ehrenberg, H. Crespi: Proc. Natl. Acad. Sci. U.S.A. 25 4642 (1978).ADSCrossRefGoogle Scholar
  22. 22.
    M. A. Marcus, A. Lewis: Biochemistry 17, 4722 (1978).CrossRefGoogle Scholar
  23. 23.
    T. Ogurusu, A. Maeda, J. Sasaki, T. Yoshizawa: Biochim. Biophys. Acta 682 446 (1982).CrossRefGoogle Scholar
  24. 24.
    S. O. Smith, M. J. Marvin, R. A. Bogomolni, R. A. Mathies: J. Biol. Chem. 259 12326 (1984).Google Scholar
  25. 25.
    T. Alshuth, M. Stockburger, P. Hagemann, D. Oesterhelt: FEBS Lett. 79 55 (1985).CrossRefGoogle Scholar
  26. 26.
    J. K. Lanyi, V. Vodyanoy: Biochemistry, 25, 1465 (1986).CrossRefGoogle Scholar
  27. 27.
    B. Schobert, J. K. Lanyi, E. J. Cragoe, Jr.: J. Biol. Chem. 258 15158 (1983).Google Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 1987

Authors and Affiliations

  • T. Ogura
    • 1
  • A. Maeda
    • 2
  • M. Nakagawa
    • 1
  • T. Kitagawa
    • 1
  1. 1.Institute for Molecular ScienceOkazaki National Research InstitutesMyodaiji, Okazaki 444Japan
  2. 2.Department of Biophysics, Faculty of ScienceKyoto UniversitySakyo-ku, Kyoto 606Japan

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