The PsbQ' protein affects the redox potential of the QA in photosystem II
| Autor: | Y. Arai, Masako Iwai, Tatsuya Tomo, A. Makita, Ryo Nagao, Masato Yamada, Hisataka Ohta |
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| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Positive shift Photoinhibition 030102 biochemistry & molecular biology Photosystem II Physiology food and beverages Plant physiology macromolecular substances Plant Science Photosynthesis Redox 03 medical and health sciences chemistry.chemical_compound 030104 developmental biology chemistry Chlorophyll Redox titration Biophysics |
| Zdroj: | Photosynthetica. 56:185-191 |
| ISSN: | 1573-9058 0300-3604 |
| DOI: | 10.1007/s11099-018-0778-8 |
| Popis: | Red alga contains four extrinsic proteins in photosystem II (PSII), which are PsbO, PsbV, PsbU, and PsbQ′. Except for the PsbQ′, the composition is the same in cyanobacterial PSII. Reconstitution analysis of cyanobacterial PSII has shown that oxygen-evolving activity does not depend on the presence of PsbQ′. Recently, the structure of red algal PSII was elucidated. However, the role of PsbQ′ remains unknown. In this study, the function of the acceptor side of PSII was analyzed in PsbQ′-reconstituted PSII by redox titration of QA and thermoluminescence. The redox potential of QA was positively shifted when PsbQ′ was attached to the PSII. The positive shift of QA is thought to cause a decrease in the amount of triplet chlorophyll in PSII. On the basis of these results, we propose that PsbQ′ has a photoprotective function when irradiated with strong light. |
| Databáze: | OpenAIRE |
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