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A New Intermediate in the Photocycle of Bacteriorhodopsin

  • R. Diller
  • M. Stockburger
Part of the Springer Proceedings in Physics book series (SPPHY, volume 20)

Abstract

The retinal-binding protein Bacteriorhodopsin in the purple membrane of Halobacteria acts as a “light-driven proton pump”. This function is controlled by a chromophoric group which contains a retinal molecule. This is bound to a lysine residue of the protein via a Schiff Base (SB) linkage. On illumination the chromophore runs through various intermediate states and under normal conditions is reconstituted within a few milliseconds. This photochemically induced and completely reversible reaction (photocycle) initiates the proton pumping mechanism /1/.

Keywords

Pump Beam Cyclic Reaction Protein State Resonance Raman Purple Membrane 
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. 1.
    D. Oesterhelt, W. Stoeckenius: Proc. Natl. Acad. Sci., USA 70, 2853 (1974) W. Stoeckenius, R.A. Bogomolni: Ann. Rev. Biochem. 51, 587 (1982)ADSCrossRefGoogle Scholar
  2. 2.
    R.H. Lozier, R.A. Bogomolni, W. Stoeckenius: Biophys.J. 15, 955 (1975)CrossRefGoogle Scholar
  3. 3.
    S.O. Smith, J. Lugtenburg, R.A. Mathies: J. Membrane Biol. 85, 95 (1985)CrossRefGoogle Scholar
  4. 4.
    M. Stockburger, T. Alshuth, D. Oesterhelt, W. Gärtner: In Advances of Spectroscopy, ed. by R.J.H. Clark and R.E. Hester, Vol. 13, Spectroscopy of Biological Systems, J. Wiley a. Sons, (1986) p. 483Google Scholar
  5. 5.
    T. Alshuth, M. Stockburger: Photochem. Photobiol. 43, 55 (1986)CrossRefGoogle Scholar
  6. 6.
    U. Fischer, D. Oesterhelt: Biophys. J. 28, 211 (1979) M. Engelhard, K. Gerwert, B. Hess, W. Kreutz, F. Siebert: Biochemistry 24, 400 (1985)CrossRefGoogle Scholar
  7. 7.
    P. Hildebrandt, M. Stockburger: Biochemistry 6, 5539 (1984)CrossRefGoogle Scholar
  8. 8.
    P. Tavan, K. Schulten: Biophys. J. 50, 81 (1986)CrossRefGoogle Scholar
  9. 9.
    W.V. Sherman, R.R. Eicke, S.R. Stafford, F.M. Wasacz: Photochem. Photobiol. 30, 727Google Scholar
  10. 10.
    W. Mäntele: Ph.D. Thesis, University of Freiburg, Freiburg, F.R.G. (1982)Google Scholar
  11. 11.
    T. Alshuth: Ph.D. Thesis, University of Göttingen, Göttingen, F.R.G. (1985)Google Scholar
  12. 12.
    Q. Li, R. Govindjee, T.G. Ebrey: Proc. Natl. Acad. Sci. USA, 81, 7079 (1984)ADSCrossRefGoogle Scholar
  13. 13.
    S.O. Smith, J.A. Pardoen, P.P.J. Mulder, B. Curry, J. Lugtenburg, R. Mathies: Biochemistry 22, 6141 (1983)CrossRefGoogle Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 1987

Authors and Affiliations

  • R. Diller
    • 1
  • M. Stockburger
    • 1
  1. 1.Max-Planck-Institut für Biophysikalische ChemieGöttingenFed. Rep. of Germany

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