The action of methyl viologen (MV) on pumpkin leaves (Cucurbita pepo L.) increased the content of reactive oxygen species (ROS) that caused disruption of the PSII electron transport chain. After the treatment by MV the seedlings were treated by protein synthesis inhibitor — chloramphenicol (CAP). The millisecond delay fluorescence of chlorophyll (Chl) a induction curves analysis (msec-DF Chl a) is shown the change of intensity of phase of msec-DF Chl a, possible in result of suppression D1 protein de novo formation. The changes of proteins profiles especially of PSII polypeptides content in chloroplasts in dependence on action of methyl viologen and chloramphenicol were observed. The high correlation between changes of PSII polypeptides and changing of stationary phase of msec-DF Chl a were shown.
Keywords: Cucurbita pepo L., oxidative damage, millisecond delay fluorescence of Chl a, reactive oxygen species, methylviologen
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1. Alonso, Z., Mun, H.C., Warwick, H., Wah, S.C. & Shunichi, T. (2015). Photodamage to the oxygen evolving complex of photosystem II by visible light. Sci. Rep., 5, p. 16363. https://doi.org/10.1038/srep16363
2. Baishnab, C.T. & Ralf, O. (2012). Reactive oxygen species generation and signaling in plants. Plant Signaling & Behavior, 7 (12), pp. 1621-1633. https://doi.org/10.4161/psb.22455
3. Jafarova, J., Ganiyeva, R., Bayramova, S. & Gasanov, R. (2019). The nature of PSII reactions stability under oxidative stress. Bangladesh J. Bot., 48 (4), pp. 1029-1035. https://doi.org/10.3329/bjb.v48i4.49051
4. Ganiyeva, R.A., Kurbanova, I.M. & Dadasheva, S.B. (2000). Fluorescence of chlorophyll and polypeptide composition of thylakoids under action of NaCl and polyethyleneglycol on wheat seedlings. Physiology and biochemistry of cultured plants, 32 (4), pp. 273-278.
5. Ganieva, R.A. & Kurbanova, I.M. Stabilization of photosynthetic membranes by polystymuline K under salt stress conditions. Physiology and biochemistry of cultured plants, 2007, 39 (4), pp. 303-310.
6. Gasanov, R.A., Alieva, S., Arao, S., Ismailova, A., Katsuta, N., Kitade, H., Yamada, Sh., Kawamori, A. & Mamedov, F. (2007). Comparative study of the water oxidizing reactions and the millisecond delayed chlorophyll fluorescence in photosystem II at different pH. J. of Photochem. Photobiol., 86, pp. 160-164. https://doi.org/10.1016/j.jphotobiol.2006.08.008
7. Gaziyev, A., Aliyeva, S., Kurbanova, I., Ganiyeva, R., Bayramova, S. & Gasanov, R. (2011). Molecular operation of metals into the function and state of photosystem II. Metallomics, 3 (12), pp. 1362-1367. https://doi.org/10.1039/c1mt00100k
8. Nishiyama, Y., Allakhverdiev, S. & Murata, N. (2011). Protein synthesis is the primary target of reactive oxygen species in the photoinhibition of photosystem II. Physiol. Plant, 142, pp. 35-46. https://doi.org/10.1111/j.1399-3054.2011.01457.x
9. Oguchi, R., Terashima, I., & Chow, W.S. (2021). The effect of different spectral light quality on the photoinhibition of Photosystem I in intact leaves. Photosynthesis Research, 149, pp 83-92. https://doi.org/10.1007/s11120-020-00805-z
10. Pathak, Vinay, Prasad, A. & Pospisil P. (2017). Formation of singlet oxygen by decomposition of protein hydroperoxide in photosystem II. PLoS One, 12 (7), p. e0181732. https://doi.org/10.1371/journal.pone.0181732
11. Kodru, S., Rehman, A. & Vass, I. (2020). Chloramphenicol enhances Photosystem II photodamage in intact cells of the cyanobacterium Synechocystis PCC 6803. Photosynthesis Research, 145, pp. 227-235. https://doi.org/10.1007/s11120-020-00784-1
12. Kolupaev, Yu.E. & Kokorev, A.I. (2019). Antioxidant system and plant resistance to water deficit. Fiziol. rast. genet., 2019, 51 (1), pp. 28-54. https://doi.org/10.15407/frg2019.01.028
13. Pavel, P. (2016). Production of Reactive Oxygen Species by Photosystem II as a Response to Light and Temperature Stress. Front Plant Sci., 7, p. 1950. https://doi.org/10.3389/fpls.2016.01950
14. Rantala, S., J¬rvi, S. & Aro, E.-M. (2021). Photosynthesis | Photosystem II: Assembly and Turnover of the Reaction Center D1 Protein in Plant Chloroplasts. Encyclopedia of Biological Chemistry III (Third Edition), pp. 207-214. https://doi.org/10.1016/B978-0-12-809633-8.21404-0
15. Renger, G. & Renger, T. (2008). Photosystem II: the machinery of photosynthetic water splitting. Photosynthesis Research, 98,(1-3), pp. 53-80. https://doi.org/10.1007/s11120-008-9345-7
16. Takahashi, Sh. & Murata, N. (2008). How do environmental stresses accelerate photoinhibition. Trends Plant Sci., 13 (4), pp. 178-182. https://doi.org/10.1016/j.tplants.2008.01.005
17. Takahashi, Sh. & Badger, M.R. (2010). Photoprotection in plants: a new light on photosystem II damage. Trends Plant Sci., 16 (1), pp. 53-60. https://doi.org/10.1016/j.tplants.2010.10.001
18. Vass, I. & Cser, K. (2009). Janus-faced charge recombinations in photosystem II photoinhibition. Trends Plant Sci., 14, pp. 200-205. https://doi.org/10.1016/j.tplants.2009.01.009
19. Vass, I. (2012). Molecular mechanisms of photodamage in the Photosystem II complex. Biochim. Biophys. Acta, 1817, pp. 209-217. https://doi.org/10.1016/j.bbabio.2005.04.003