Advertisement

Photosynthesis pp 289-304 | Cite as

The Stable Primary Electron Acceptor QA and the Secondary Electron Acceptor QB

Part of the Advances in Photosynthesis and Respiration book series (AIPH, volume 10)

Keywords

Fluorescence Yield Spinach Chloroplast Bacterial Reaction Center Primary Electron Acceptor Photosynthetic 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.

For further reading

  1. R1.
    BA Diner and GT Babcock (1996) Structure, dynamics, and energy conversion efficiency in photosystem II. In: DR Ort and CF Yocum (eds) Oxygenic Photosynthesis: The Light Reactions, pp 213–247. KluwerGoogle Scholar
  2. R2.
    BA Diner, V Petrouleas and JJ Wendoloski (1991) The iron-quinone-acceptor complex of photosystem II. Phyiol Plant 81: 423–436Google Scholar
  3. R3.
    Irmgard Sinning (1992) Herbicide binding in the bacterial photosynthetic reaction center. Trends Biochem Sci 17: 150–154PubMedCrossRefGoogle Scholar

References

  1. 1.
    LNM Duysens and HE Sweers (1963) Mechanism of the two photochemical reactions in algae as studied by means of fluorescence: In: Studies on Microalgae and Photosynthetic Bacteria (Japanese Soc. Plant Physiologists, ed) pp 353–372. Univ Tokyo Press, TokyoGoogle Scholar
  2. 2.
    Nl Bishop (1959) The reactivity of a naturally occurring quinone (Q-255) in photochemical reactions of isolated chloroplasts. Proc Nat Acad Sci, USA 45: 1696–1702Google Scholar
  3. 3.
    HH Stiehl and HT Witt (1968) Die kurzzeitigen ultravioletten Differenzspektren bei der Photosynthese. Z Naturforsch 23b: 220–224Google Scholar
  4. 4.
    HJ van Gorkom (1974) Identification of the reduced primary electron acceptor of photosystem II as a bound semiquinone anion. Biochim Biophys Acta 347: 439–442PubMedGoogle Scholar
  5. 5.
    DB Knaff and Dl Arnon (1969) Spectral evidence for a new photoreactive component of the oxygen-evolving system in photosynthesis. Proc Nat Acad Sci, USA 63 963–969Google Scholar
  6. 6.
    S Gerken, JP Dekker, E Schlodder and HT Witt (1989) Studies on the multiphasic charge recombination between chlorophyll aii+(P680+) and plastoquinone QA-in photosystem II complexes. Ultraviolet difference spectrum in Chi-aii+/Chi-aii Biochim Biophys Acta 977: 55, 56Google Scholar
  7. 7.
    WA Cramer and WL Butler (1969) Potentiometric titration of the fluorescence yield of spinach chloroplasts. Biochim Biophys Acta 172: 503–510PubMedGoogle Scholar
  8. 8.
    P Horton and E Croze (1979) Characterization of two quenchers of chlorophyll fluorescence with different midpoint oxidation-reduction potentials in chloroplasts. Biochim Biophys Acta 545: 188–201PubMedGoogle Scholar
  9. 9.
    B Ke, FM Hawkridge and S Sahu (1976) Redox titration of fluorescence yield of photosystem II. Proc Nat Acad Sci, USA 73: 2211–2215Google Scholar
  10. 10.
    DB Knaff (1975) The effect of pH on the midpoint oxidation-reduction potentials of components associated with plant photosystem II. FEBS Lett 60: 331–335CrossRefGoogle Scholar
  11. 11.
    A Vermeglio (1977) Secondary electron transfer in reaction centers of Rhodopseudomonas sphaeroides. Out-of-phase periodicity of two for the formation of ubisemiquinone and fully reduced ubiquinone. Biochim Biophys Acta 459: 516–524PubMedGoogle Scholar
  12. 12.
    CA Wraight (1977) Electron acceptors of photosynthetic bacterial reaction centers. Direct observation of oscillatory behaviour suggesting two closely equivalent ubiquinones. Biochim Biophys Acta 459: 525–531PubMedGoogle Scholar
  13. 13.
    B Bouges-Bocquet (1973) Electron transfer between two photosystems in spinach chloroplasts. Biochim Biophys Acta 314: 250–256PubMedGoogle Scholar
  14. 14.
    BR Velthuy and J Amesz (1974) Charge accumulation at the reducing side of photosystem 2 of photosynthesis. Biochim Biophys Acta 333: 85–94Google Scholar
  15. 15.
    AW Rutherford and P Mathis (1983) A relationship between the midpoint potential of the primary acceptor and low temperature photochemistry in photosystem II. FEBS Lett 154: 328–334CrossRefGoogle Scholar
  16. 16.
    W Klimov, E Dolan, ER Shaw and B Ke (1980) Interaction between the intermediary electron acceptor (pheophytin) and a possible plastoquinone-iron complex in photosystem-ll reaction centers. Proc Nat Acad Sci, USA 77: 7227–7231Google Scholar
  17. 17.
    H Michel and J Deisenhofer (1988) Relevance of the photosynthetic reaction center from purple bacteria to the structure of photosystem II. Biochemistry 27: 1–7CrossRefGoogle Scholar
  18. 18.
    JJS van Rensen, C.H Xu and Govindjee (1999) Role of bicarbonate in photosystem II, the water-plasto-quinone oxido-reductase of plant photosynthesis. Physiol Plant 105: 585–592Google Scholar
  19. 19.
    CA Wraight (1988) The involvement of stable semiquinones in the two electron gates of plant and bacterial photosynthesis. In: B Trumpower (ed) Function of Quinones in Energy-Conserving Systems, pp 181–197Google Scholar
  20. 20.
    BR Velthuy (1988) Electron-dependent competition between plastoquinone and inhibitors for binding to photosystem II. FEBS Lett 126: 277–281Google Scholar
  21. 21.
    H Michel, O Epp and J Deisenhofer (1986) Pigment-protein interactions in the photosynthetic reaction centre from Rhodopseudomonas viridis. EMBO J 5: 2445–2451Google Scholar
  22. 22.
    ML Paddock, SH Rongey, EC Abresch, G Feher and MY Okamura (1988) Reaction centers from three herbi-cide-resistant mutants of Rhodobacter sphaeroides 2.4.2: sequence analysis and preliminary characterization. Photosynthesis Res 17: 75–96Google Scholar
  23. 23.
    I Sinning, H Michel, P Mathis and AW Rutherford (1989) Terbutryn resistance in a purple bacterium can induce sensitivity toward plant herbicide DCMU. FEBS Lett 256: 192–194CrossRefGoogle Scholar
  24. 24.
    I Sinning, J Koepke and H Michel (1990) Recent advances in the structure analysis of Rhodopseudomonas viridis mutants. In M.E Michel-Beyerle (ed) Springer Series in Biophysics, Vol 6, Reaction Centers of Photosynthetic Bacteria, pp 199–208Google Scholar

Copyright information

© Kluwer Academic Publishers 2003

Personalised recommendations