Photoinhibition of Electron Transport Activity of Photosystem II in Isolated Thylakoids Studied by Thermoluminescence and Delayed Luminescence

  • Imre Vass
  • Narendranath Mohanty
  • Sándor Demeter
Part of the NATO ASI Series book series (NSSA, volume 168)


Photosynthetic organisms exposed to higher light intensity than that required to saturate photosynthesis gradually lose their photosyn-thetic capacity. The phenomenon is called photoinhibition and related to a damage in photosystem II (PS II) [1–5]. However, the opinions differ concerning the exact site of photodamage. Works using algae cells suggest that the QB binding protein is injured [2,9]. On the other hand the majority of experiments on isolated chloroplasts advocate a primary site of photoinhibition in the P680-Pheo-QA section of the electron transport chain [3–5]. Recently thermoluminescence (TL) and delayed luminescence (DL) proved to be useful methods in the investigation of PS II photochemistry. Well characterized TL and DL signals are arising from the S2QA and S2QB charge recombinations [6–8]. Thus it is expected that the effect of photoinhibition on the QA and QB acceptors can be easily followed by these techniques. Recent TL investigation of photoinhibition in Chlamydomonas reinhardii cells led to the conclusion that in the first stage of photoinhibition the QB binding site is modified while the QA acceptor is only slightly influenced [9]. Considering that in isolatea thylakoids the process of photoinhibition may differ from that occurring in intact cells we carried out TL and DL measurements of photoinhibited spinach thylakoids.


Electron Transport Chain Alga Cell High Light Intensity Electron Transport Rate Charge Recombination 


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  1. 1.
    S.B. Powles, Photoinhibition of photosynthesis induced by visible light, Annu. Rev. Plant. Physiol. 35:15 (1984)CrossRefGoogle Scholar
  2. 2.
    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)PubMedCrossRefGoogle Scholar
  3. 3.
    B. Arntz and A. Trebst, On the role of the QB protein in PS II in photoinhibition, FEBS Lett. 194:43 (1986)CrossRefGoogle Scholar
  4. 4.
    R.E. Cleland, A. Melis and P.J. Neale, Mechanism of photoinhibi-tion: photochemical reaction center inactivation in system II of chloroplasts, Photosynthesis Res. 9:79 (1986)CrossRefGoogle Scholar
  5. 5.
    S.I. Allakhverdiev, E. Setlikova, V.V. Klimov and I. Setlik, In photoinhibited photosystem II particles pheophytin photoreduction remains unimpaired, FEBS Lett. 226:186 (1987)CrossRefGoogle Scholar
  6. 6.
    A.W. Rutherford, A.R. Crofts and Y. Inoue, Thermoluminescence as a probe of photosystem II photochemistry. The origin of the flash-induced glow peaks, Biochim. Biophys. Acta 682, 457–465 (1982)CrossRefGoogle Scholar
  7. 7.
    S. Demeter and I. Vass, Charge accumulation and recombination in photosystem II studied by thermoluminescence. I. Participation of the primary acceptor Q and secondary acceptor B in the generation of thermoluminescence of chloroplasts, Biochim. Biophys. Acta 764:24 (1984)CrossRefGoogle Scholar
  8. 8.
    É. Hideg and S. Demeter, Binary oscillation of delayed luminescence: Evidence of the participation of QB in the charge recombination, Z. Naturforsch. 40c:827 (1985)Google Scholar
  9. 9.
    I. Ohad, H. Koike, S. Shochat and Y. Inoue, Changes in the properties of reaction center II during the initial stages of photoinhibition as revealed by thermo luminescence measurements, Biochim. Biophys. Acta 933:288 (1988)CrossRefGoogle Scholar
  10. 10.
    O. Nanba and K. Satoh, Isolation of a photosystem II reaction center consisting of D-1 and D-2 polypeptides and cytochrome b-559, Proc. Natl. Acad. Sci. USA 84:109 (1987)PubMedCrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1989

Authors and Affiliations

  • Imre Vass
    • 1
  • Narendranath Mohanty
    • 1
  • Sándor Demeter
    • 1
  1. 1.Institute of Plant PhysiologyBiological Research Center of the Hungarian Academy of SciencesSzegedHungary

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