Advertisement

Time-Resolved FTIR Difference Spectroscopy of Photosynthetic Bacterial Reaction Centers

  • D. L. Thibodeau
  • E. Nabedryk
  • R. Hienerwadel
  • F. Lenz
  • W. Mäntele
  • J. Breton
Part of the Springer Proceedings in Physics book series (SPPHY, volume 68)

Abstract

Primary photosynthetic reactions feature rapid kinetics with high quantum yield of stable charge separation occurring in basic units called reaction centers (RC). The X-ray structure of bacterial RC [1,2] suggests that the efficiency and the stability of the charge separation rely at least partly on the protein environment to optimize the orientation and the localization of the various redox components involved in electron transport. The differences in the nature and organization of the aminoacids forming the binding pocket of the two quinones, QA and QB, are thought to be responsible for their different properties in JRC. Indeed, the two quinones are unequivalent, QA (menaquinone for Rps. viridis and ubiquinone for Rb. sphaeroides) is more tightly bound to the protein than QB (ubiquinone for both RC), and they display different redox properties i.e. QA is a one-electron acceptor while QB can accept two electrons under physiological conditions.

Keywords

Reaction Center Difference Spectrum Protein Environment Acceptor Quinone Bacterial Reaction Center 
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.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    H. Michel, O. Epp, J. Deisenhofer: EMBO J. 5, 2445 (1986)Google Scholar
  2. 2.
    J.P. Allen, G. Feher, T.O. Yeates, H. Komiya, D.C. Rees: Proc. Natl Acad. Sci. USA 85, 8487 (1988)ADSCrossRefGoogle Scholar
  3. 3.
    R.J. Shopes, C.A. Wraight: Biochim. Biophys. Acta 806, 348–356 (1985)CrossRefGoogle Scholar
  4. 4.
    R.K. Clayton, H.F. Yau: Biophys. J. 12, 867 (1972)CrossRefGoogle Scholar
  5. J.R. Codgell, D.C. Brune, RK. Clayton: FEES Lett 45, 344 (1974)CrossRefGoogle Scholar
  6. 5.
    W. Mäntele, A. Wollenweber, E. Nabediyk, J. Breton: Proc. Natl Acad. Sci. USA 85, 8468 (1988)ADSCrossRefGoogle Scholar
  7. 6.
    E. Nabedryk, KA. Bagley, D.L. Thibodeau, M. Bauscher, W. Mantele, J. Breton: FEBS Lett 266, 59 (1990)CrossRefGoogle Scholar
  8. 7.
    D.L. Thibodeau, E. Nabedryk, R. Hienerwadel, F. Lenz, W.G. Mantele, J. Breton: Biochim. Biophys. Acta 1020, 253 (1990)CrossRefGoogle Scholar
  9. 8.
    D.L. Thibodeau, J. Breton, C. Berthomieu, KA. Bagley, W. Mantele, E. Nabedfyk: Bacterial Reaction Centers, Structure and Dynamics (Springer Series in Biophysics, Berlin, 1990) vol. 6, pp. 87–989.Google Scholar
  10. 9.
    J. Breton, D.L Thibodeau, C. Berthomieu, W.G. Mäntele, A Verméglio, E. Nabediyk: FEBS Letters 278, 257 (1991)CrossRefGoogle Scholar
  11. J. Breton, C. Berthomieu, D.L. Thibodeau, E. Nabedryk (in preparation) (1991)Google Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 1992

Authors and Affiliations

  • D. L. Thibodeau
    • 1
  • E. Nabedryk
    • 1
  • R. Hienerwadel
    • 1
  • F. Lenz
    • 2
  • W. Mäntele
    • 2
  • J. Breton
    • 1
  1. 1.SBE/DBCMCEN SaclayGif-sur-Yvette CedexFrance
  2. 2.Institut für BiophysikUniversität FreiburgFreiburgFed. Rep. of Germany

Personalised recommendations