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'Photoinhibition' in keywords Facet   section ZfN Section C:Volume 043  [X]
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1988 (2)
1Author    Imre Vass, Narendranath Mohanty, Sándor DemeterRequires cookie*
 Title    Photoinhibition of Electron Transport Activity of Photosystem II in Isolated Thylakoids Studied by Thermoluminescence and Delayed Luminescence  
 Abstract    The effect of photoinhibition on the primary (Oa) and secondary (Ob) quinone acceptors of photosystem II was investigated in isolated spinach thylakoids by the methods of thermolumines-cence and delayed luminescence. The amplitudes of the Q (at about 2 °C) and B (at about 30 °C) thermoluminescence bands which are associated with the recombination of the S;OA and S2QB charge pairs, respectively, exhibited parallel decay courses during photoinhibitory treatment. Similarly, the amplitudes of the flash-induced delayed luminescence components ascribed to the recombination of S 2 0A and S 2 OB charge pairs and having half life-times of about 3 s and 30 s, respectively, declined in parallel with the amplitudes of the corresponding Q and B thermo-luminescence bands. The course of inhibition of thermoluminescence and delayed luminescence intensity was parallel with that of the rate of oxygen evolution. The peak positions of the B and Q thermoluminescence bands as well as the half life-times of the corresponding delayed lumines-cence components were not affected by photoinhibition. These results indicate that in isolated thylakoids neither the amount nor the stability of the reduced OB acceptor is preferentially decreased by photoinhibition. We conclude that either the primary target of photodamage is located before the Ob binding site in the reaction center of photosystem II or QA and OB undergo simultaneous damage. 
  Reference    Z. Naturforsch. 43c, 871—876 (1988); received August 12 1988 
  Published    1988 
  Keywords    Photosynthesis, Photoinhibition, Photosystem II, Thermoluminescence, Delayed Luminescence 
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 TEI-XML for    default:Reihe_C/43/ZNC-1988-43c-0871.pdf 
 Identifier    ZNC-1988-43c-0871 
 Volume    43 
2Author    Matthias Kuhn, Andreas Thiel, Peter BögerRequires cookie*
 Title    The 9-kDa Phosphoprotein Involved in Photoinhibition  
 Abstract    Photosystem-II particles exhibit strong photoinhibition. Short-term illumination of photosys-tem-II particles with high-intensity light (5000 piE/m 2 x s) leads to a typical change of the protein pattern on SDS-PAGE. Two proteins are mainly affected, namely the well-described 32-kDa herbicide-binding protein which probably is degraded [1] and, first published here, the 9-kDa phosphoprotein, whose function in the PS-II complex is still unknown. This protein is not de-graded, but seems to be linked to other polypeptides of the PS-II complex. During light treatment new bands of 23, 41, 50 and 54 kDa appear in the protein pattern of SDS-PAGE. A monospecific antiserum was produced against the 9-kDa phosphoprotein to investigate its fate. After light treatment the antibodies reacted with new proteins of higher molecular weights, most pronounced with a 23-kDa and a 41-kDa peptide. 
  Reference    Z. Naturforsch. 43c, 413—417 (1988); received February 15 1988 
  Published    1988 
  Keywords    9-kDa Phosphoprotein, Photosystem-II Particles, Photoinhibition, Protein Phosphorylation, Antibody 
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 TEI-XML for    default:Reihe_C/43/ZNC-1988-43c-0413.pdf 
 Identifier    ZNC-1988-43c-0413 
 Volume    43