Damaging Processes in the Reaction Center and on Its Acceptor Side During Photoinactivation of PSII Particles

  • Ladislav Nedbal
  • Jiři Masojidek
Part of the NATO ASI Series book series (NSSA, volume 168)


The photoinactivation of photosystem II is a very complex process which gradually affects all of its parts. A damage has been reported to occur in the reaction center itself /P680-Pheo/1,2,3,4 as wetl as on its donor /Z,D,Mn/S-states/5,6 and acceptor /QA,QB/7,8.9,10 sides. It is not clear, yet, where the photoinactivat ion starts, in what order the secondary processes occur and what the underlying mechanism of the damage is. These questions are addressed also in the present paper.


Acceptor Side Primary Charge Separation Chlorophyll Protein PSII Particle Constant Fluorescence 


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  1. 1.
    B. Arntz and A. Trebst, On the role of the QB protein of PSII in photoinhibition, FEBS Lett, 194:43 /1986/CrossRefGoogle Scholar
  2. 2.
    S. Demeter, P. J. Neale and A. MeLis. Photoinhibition: Impairment of the primary charge separation between P680 and pheophytin in PSII of chlorop Lasts, FEBS Lett, 214:370 /1987/CrossRefGoogle Scholar
  3. 3.
    K. Satoh and D. C. Fork, Photoinhibition of reaction centers of photosystems I and II in intact Bryopsi s chloroplasts under anaerobic conditions. Plant Physiol. 70:1004 /1982/PubMedCrossRefGoogle Scholar
  4. 4.
    R. E. Cleland and C Critchley, Studies on the mechanism of photoinhibition in higher plants. Inactivation by high light of PSII reaction center function in isolated chloroplasts, Photobiochem. Photobiophys. 10:83 /1985/Google Scholar
  5. 5.
    F.E. Callahan and G.M. Cheniae, Studies on the photoactivation of the water-oxidazing enzyme. I. Processes limiting photoactivation in hydroxylamin-extracted leaf segments, Plant Physiol. 79:777 /1985/PubMedCrossRefGoogle Scholar
  6. 6.
    S. M. Theg, L. J. Filar and R. A. Dilley, Photoinactivat ion of chloroplasts already inhibited on the oxidizing side of PSII, Biochim, Biophys. Acta 849:104 /1986/CrossRefGoogle Scholar
  7. 7.
    L. Nedbal, E. Šetlíková, J. Masojídek and I. Šetlik, The nature of photoinhibition in isolated thylakoids, Biochim, Biophys. Acta 848:108 /1986/CrossRefGoogle Scholar
  8. 8.
    A. Allakhverdiev, E. Šetlíková, V. V. Klimov and I. Šetlik, In photoinhibited PSII particles pheophytin photoreduction remains unimpaired, FEBS Lett, 226:186 /1987/CrossRefGoogle Scholar
  9. 9.
    D. J. Kyle, I. Ohad and C. J. Arntzen, Membrane protein damage and repair: selective loss of a quinone protein function in chloroplast membranes, Proc, Natl, Acad, Sci, USA 81:4070 /1984/CrossRefGoogle Scholar
  10. 10.
    A. K. Mattoo, H. Hoffman-Falk, J. B. Marder and M. Edelman, Regulation of protein metabolism: coupling of photosynthetic electron transport to in vivo degradation of the rapidly metabolized 32-kD protein, Proc, Natl, Acad, Sei-USA 81:1380 /1984/CrossRefGoogle Scholar
  11. 11.
    N. I. Shutilova, V. V. Klimov, V. A. Shuvalov and V. M. Kutyurin, Isolation and investigation of photochemical and spectral properties of PSII subchlorplast fragments which are highly purified from PSI admixtures, Biofizika /russ-/ 20:844 /1975/Google Scholar
  12. 12.
    O. Machold, Relationship between the 43 kDa chlorophyll protein of PSII and the rapidly metabolized 32 kDa QB protein, FEBS Lett. 204:363 /1986/CrossRefGoogle Scholar
  13. 13.
    U. K. Laemmli, Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227:680 /1970/PubMedCrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1989

Authors and Affiliations

  • Ladislav Nedbal
    • 1
  • Jiři Masojidek
    • 1
  1. 1.Institute of MicrobiologyCzechoslovak Academy of SciencesTřebonCzechoslovakia

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