Advertisement

Structural and Functional Properties of the Isolated Photosystem Two Reaction Centre

  • J. Barber
  • D. J. Chapman
  • K. Gounaris
  • J. B. Marder
  • A. Telfer
Part of the NATO ASI Series book series (NSSA, volume 168)

Abstract

The sequencing of the genes for the L and M subunits of the purple bacterial reaction centre and the D1 and D2 polypeptides of photosystem two (PS2) revealed striking homologies in localized areas (1,2). The likely meaning of these homologies emerged from the X-ray crystallography work of Deisenhofer et al (3) using crystals of the isolated reaction centre of Rhodopseudomonas viridis. Such a comparison indicated that like the L and M polypeptides, the D1 and D2 polypeptides probably form the heart of the PS2 reaction centre (4–6). This prediction was supported by work of Nanba and Satoh (7) who isolated a chlorophyll binding complex from spinach chloroplasts consisting only of the D1, D2 and cytochrome b559 polypeptides which were able to catalyse photoreactions indicative of the PS2 reaction centre. Using pea rather than spinach, we also isolated a D1/D2/cyt b559 complex which we have subjected to detailed structural and functional analysis. Here we summarise our findings.

Keywords

Reaction Centre Chlorophyll Fluorescence Cytochrome B559 Photosynthetic Reaction Centre Reaction Centre Complex 
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.
    J.E. Hearst and K. Sauer, Protein sequence homologies between positions of the L and M subunits of reaction centres of Rhodopseudomonas capsulata and the QB protein of chloroplast thylakoid membranes: proposed relation to quinone-binding sizes, Z. fur Naturforsch 39:421–424 (1984)Google Scholar
  2. 2.
    J.C. Williams, L.A. Steiner, G. Feher and M.I. Simon, Primary structure of the L subunit of the reaction cnetre from Rhodopseudomonas sphaeroides. Proc. Natl. Acad. Sci USA 81:7303–7307(1984)Google Scholar
  3. 3.
    J. Deisenhofer, O. Epp, K. Miki, R. Huber and H. Michel, Structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3 A° resolution, Nature 318:618–624 (1985)PubMedCrossRefGoogle Scholar
  4. 4.
    H. Michel and J. Deisenhofer, The relevance of the photosynthetic reaction centre from purple bacteria to the structure of photosystem II, Biochemistry 27:1–7(1988)CrossRefGoogle Scholar
  5. 5.
    A. Trebst, The topology of the plastoquinone and herbicide binding peptides of photosystem two in the thylakoid membrane, Z. fur Naturforsch 41c:240–245 (1986)Google Scholar
  6. 6.
    J. Barber and J.B. Marder, Application of molecular genetics for determining photosynthetic membrane structure, in: Biotech. Genet. Eng. Revs. Vol.4, pp355–404, Intercept Ltd., Newcastle, UK (1986)Google Scholar
  7. 7.
    O. Nanba and K. Satoh, Isolation of a photosystem two reaction centre containing D1 and D2 polypeptides and cytochrome b559, Proc. Natl. Acad. Sci. USA, 84:109–112(1987)PubMedCrossRefGoogle Scholar
  8. 8.
    D. J. Chapman, K. Gounaris and J. Barber, Electron transport properties of the isolated D1/D2 cytochrome b559 photosystem two reaction centre, Biochim. Biophys. Acta 933:423–431 (1988)CrossRefGoogle Scholar
  9. 9.
    D.A. Berthold, G.T. Babcock and C.F. Yocum, A highly resolved O2 evolving PSII preparation from spinach thylakoid membranes, FEBS Lett. 134:231–234 (1981)CrossRefGoogle Scholar
  10. 10.
    J.B. Marder, D.J. Chapman, A. Telfer, Identification of psb A and psb B gene products, D1 and D2, as reaction centre proteins of photosystem two, Plant Mol. Biol. 9:325–333 (1987)CrossRefGoogle Scholar
  11. 11.
    P.J. Nixon, T.A. Dyer, J. Barber and C.N. Hunter, Immunological evidence for the presence of the D1 and D2 proteins in PS2 cores of higher plants, FEBS Lett. 209:83–86(1986)Google Scholar
  12. 12.
    A.N. Webber, L. Packman, D.J. Chapman, J. Barber and J.C. Gray, The photosystem II reaction centre complex contains five polypeptides, FEBS Lett. (1989) in pressGoogle Scholar
  13. 13.
    W.R. Newell, H.van Amerongen, R. van Grondelle, R. Aalnerts, J.W. Drake, P. Udvarhelyi and J. Barber, Spectroscopic characterisation of the reaction centre of photosystem two from higher plants, FEBS Lett. 228:162–166 (1988)CrossRefGoogle Scholar
  14. 14.
    K. Gounaris, D.J. Chapman and J. Barber, The interaction between the 33 kD manganese stabilising protein and the Dl/D2/cyt b559 complex, FEBS Lett. 234:374–378(1988)Google Scholar
  15. 15.
    Y. Takahashi, P. Hansson and P. Mathis, Primary radical pair in the photosystem II reaction centre, Biochim. Biophys. Acta 893:49–59 (1988)Google Scholar
  16. 16.
    R.V. Danielius, K. Satoh, P.J.M. Van Kan, J.J. Plijter, A.M. Nuijs and H.J. Van Gorkom, The primary reaction of photosystem two in the Dl-D2-cytochrome b559 complex, FEBS Lett. 213:241–244 (1987)CrossRefGoogle Scholar
  17. 17.
    M.Y. Okamura, K. Satoh, R.A. Isaacson, and G. Feher, Evidence of the primary charge separation in the D1/D2/ complex of photosystem II in spinach: EPR of the triplet state, in: Progress in Photosynthesis Research, J. Biggins, ed., Vol.1 pp379–381, Martinus Nijhoff Publ., The Hague (1987)Google Scholar
  18. 18.
    A. Telfer, M.C.W. Evans and J. Barber, Oxidation-reduction potential dependence of reaction centre triplet formation in the isolated Dl/D2/cytochrome b559 photosystem two complex, FEBS Lett. 232:209–213 (1988)CrossRefGoogle Scholar
  19. 19.
    D. Klug, Excitons and charge separation in higher plant chromophore protein complexes. Ph.D. Thesis, University of London (1988)Google Scholar
  20. 20.
    J. Barber, D.J. Chapman and A. Telfer, Characterisation of a photosystem two reaction centre isolated from the chloroplast, FEBS Lett. 220:67–73 (1987)CrossRefGoogle Scholar
  21. 21.
    K. Gounaris, D.J. Chapman and J. Barber, Reconstitution of plastoquinone in the D1/D2/cyt b559 photosystem two reaction centre, FEBS Lett. 240:143–147 (1988)CrossRefGoogle Scholar
  22. 22.
    M.T. Giardi, J.B. Marder and J. Barber, Herbicide binding to the isolated photosystem two reaction centre, Biochim. Biophys. Acta 934:64–71 (1988)CrossRefGoogle Scholar
  23. 23.
    A. Telfer, J.B. Marder and J. Barber, Photosystem two reaction centres isolated from phosphorylated pea thylakoids carry phosphate on the D1 and D2 polypeptide subunits, Biochim. Biophys. Acta 893:557–563 (1987)CrossRefGoogle Scholar
  24. 24.
    J.B. Marder, A. Telfer and J. Barber, The Dl polypeptide subunits of the photosytem II reaction centre has a phosphorylation site at its amino terminus, Biochim. Biophys. Acta 932:362–365 (1988)CrossRefGoogle Scholar
  25. 25.
    M. Edelman, P. Goloubinoff, J.B. Marder, H. Fromm, R. Fluhr and A.K. Matoo, Structure-function relationships and regulation of the 32 kD protein in the photosynthetic membranes, in: Molecular form and function of the plant genome, L. Vloten-Doting, G.S.P. Groot and T.C. Hall, eds.) pp291–300, Plenuum Press (1985)Google Scholar
  26. 26.
    D.J. Kyle, The 32000 Dalton QR protein of photosystem II, Photochem. Photobiol. 41:107–116(1985)Google Scholar
  27. 27.
    J. Barber, S. Malkin and A. Telfer, The origin of chlorophyll fluorescence in vivo and its quenching by the photosystem two reaction centre, Proc. Roy. Soc. (London) in press (1988)Google Scholar
  28. 28.
    V.V. Klimov, A.V. Klevonik, V.A. Shuvalov and A.A. Krasnovsky, Reduction of pheophytin in the primary light reactions of photosystem II, FEBS Lett. 82:183–186(1977)PubMedCrossRefGoogle Scholar
  29. 29.
    G.H. Schatz, H. Brock and A.R. Holzwarth, Picosecond kinetics of fluorescence and absorbance changes in photosystem II particles excited at low photon density, Proc. Natl. Acad. Sci. USA, 84:8414–8418 (1987)PubMedCrossRefGoogle Scholar
  30. 30.
    I. Fujita, M.S. Davis and J. Fajer, Anion radicals of pheophytin and chlorophyll a. Their role in the primary charge separation of plant photosynthesis, J. Am. Chem. Soc. 100:6280–6282 (1978)CrossRefGoogle Scholar
  31. 31.
    J. Barber, Photosynthetic reaction centres: A common link, Trends Biochem. Sci. 12:321–326(1987)CrossRefGoogle Scholar
  32. 32.
    R.J. Debus, B.A. Barry, G.T. Babcock and L. Mcintosh, Site directed mutagenesis identifies a tyrosine radical involved in photosynthetic oxygen evolution system. Proc. Natl. Acad. Sci (USA) 85:427–430 (1988)CrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1989

Authors and Affiliations

  • J. Barber
    • 1
  • D. J. Chapman
    • 1
  • K. Gounaris
    • 1
  • J. B. Marder
    • 1
  • A. Telfer
    • 1
  1. 1.AFRC Photosynthesis Research Group, Department of Pure & Applied Biology, Technology & MedicineImperial College of ScienceLondonUK

Personalised recommendations