Photochemistry in the Isolated Photosystem 2 Reaction Centre

  • Christalla Demetriou
  • Christopher J. Lockett
  • Jonathan H. A. Nugent
Chapter
Part of the NATO ASI Series book series (NSSA, volume 168)

Abstract

The recent isolation of a complex containing the polypeptides D1, D2 and cytochrome b559, confirmed the proposal that D1 and D2 bind the reaction centre components of PS21,2. The complex was shown to be photochemically active by the photoreduction of phaeophytin and a spin polarised triplet was also detected by epr3. The triplet species originates from a radical pair recombination between the oxidised primary donor chlorophyll P680+ and the reduced phaeophytin acceptor I-4.Redox titrations of the reaction centre preparation using the spin polarised triplet signal confirmed the lack of a quinone electron acceptor but suggested that the non-haem iron still present may act as an electron acceptor when oxidised5.

Keywords

Reaction Centre Continuous Illumination Scenedesmus Obliquus Redox Titration Zero Field Split Parameter 
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.
This is a preview of subscription content, log in to check access.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    O. Nanba and K. Satoh, Proc. Natl. Acad. Sci. USA 84:109 (1987)PubMedCrossRefGoogle Scholar
  2. 2.
    M. Michel and J. Deisenhofer, Biochemistry 27: 1 (1988)CrossRefGoogle Scholar
  3. 3.
    J. Barber, D.J. Chapman and A. Teifer, FEBS Lett. 220:67 (1987)CrossRefGoogle Scholar
  4. 4.
    A.W. Rutherford, D.R. Paterson and J.E. Mullet, Biochim. Biophys. Acta 635:205 (1981)PubMedCrossRefGoogle Scholar
  5. 5.
    A. Telfer, J. Barber and M.C.W. Evans, FEBS Lett. 232:209 (1988)CrossRefGoogle Scholar
  6. 6.
    R.C. Ford and M.C.W. Evans, FEBS Lett. 160:159 (1983)CrossRefGoogle Scholar
  7. 7.
    J.G. Metz and M. Siebert, Plant Physiol. 76:829 (1984)PubMedCrossRefGoogle Scholar
  8. 8.
    N.I. Bishop, Methods Enzymol. 23:372 Academic press. New York (1971)CrossRefGoogle Scholar
  9. 9.
    M.C. Thurnauer, J.J. Katz and J.R. Norris, Proc. Natl. Acad. Sci. USA 72:3270 (1975)PubMedCrossRefGoogle Scholar
  10. 10.
    A.W. Rutherford and J.E. Mullet, Biochim. Biophys. Acta 635:225 (1981)PubMedCrossRefGoogle Scholar
  11. 11.
    H.A. Frank, M.B. McLean and K. Sauer, Proc. Natl. Acad. Sci. USA 76:5124 (1979)PubMedCrossRefGoogle Scholar
  12. 12.
    M.C. Thurnauer and J.R. Norris, Chem. Phys. Lett. 47:100 (1977)CrossRefGoogle Scholar
  13. 13.
    A.W. Rutherford and M.C. Thurnauer, Proc. Natl. Acad. Sci. USA 79:7283 (1982)PubMedCrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1989

Authors and Affiliations

  • Christalla Demetriou
    • 1
  • Christopher J. Lockett
    • 1
  • Jonathan H. A. Nugent
    • 1
  1. 1.Department of BiologyUniversity College LondonLondonUK

Personalised recommendations