Abstract
The role of D1-protein in photoinhibition was examined. Photoinhibition of spinach thylakoids at 20°C caused considerable degradation of D1-protein and a parallel loss of variable fluorescence, QB-independent electron flow and QB-dependent electron flow. The breakdown of D1-protein as well as the loss of variable fluorescence and QB-independent electron flow were largely prevented when thylakoids were photoinhibited at 0°C. The QB-dependent electron flow markedly decreased under the same conditions. This inactivation may represent the primary event in photoinhibition and could be the result of some modification at the QB-site of D1-protein. Evidence for this comes from fluorescence relaxation kinetics following photoinhibition at 0°C which indicate a partial inactivation of QA --reoxidation. These results support the idea of D1-protein breakdown during photoinhibition as a two step process consisting of an initial inactivation at the QB-site of the protein followed by its degradation. The latter is accompanied by the loss of PS II-reaction centre function.
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Abbreviations
- Asc:
-
ascorbate
- p-BQ:
-
1, 4-benzoquinone
- DAD:
-
diaminodurene
- DPC:
-
diphenylcarbazide
- DQH2 :
-
duroquinole
- Fecy:
-
ferricyanide
- MV:
-
methylviologen
- QA :
-
primary quinone acceptor of PS II
- QB :
-
secondary quinone acceptor of PS II
- SiMo:
-
silicomolybdate
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Richter, M., Rühle, W. & Wild, A. Studies on the mechanism of photosystem II photoinhibition I. A two-step degradation of D1-protein. Photosynth Res 24, 229–235 (1990). https://doi.org/10.1007/BF00032310
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DOI: https://doi.org/10.1007/BF00032310