Abstract
The redox interaction of exogenous cytochrome c550 (Cyt) with PSII isolated from spinach was studied. Illumination of PSII particles in the presence of Cyt led to: (1) Cyt photooxidation by PSII reaction center (demonstrated at the first time), (2) Cyt photoreduction via O2−• photoproduced on the acceptor side of PSII, and (3) Cyt photoreduction by reduced electron carriers of PSII. A step-by-step removal of components of water-oxidizing complex was accompanied by the appearance of Cyt photooxidation, an increase in the superoxide dismutase (SOD)-dependent Cyt photoreduction (related to O2−• formation), and a decrease in the SOD-independent Cyt photoreduction. Re-addition of PsbO protein diminished the Cyt-induced restoration of electron transfer in PSII. Addition of diuron led to inhibition of these photoprocesses, while exogenous Mn2+ inhibited only the Cyt c photooxidation. The results can be important for correct measurements of O2−• photoproduction in PSII and for elucidation of the role of cytochrome c550 in cyanobacterial PSII.
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Abbreviations
- Chl:
-
chlorophyll
- Cyt:
-
cytochrome
- DCMU:
-
3-(3,4-dichlorophenyl)-1,1-dimethylurea
- P680 :
-
the primary electron donor of PSII
- Pheo:
-
pheophytin (the primary electron acceptor of PSII)
- RC:
-
reaction center
- SOD:
-
superoxide dismutase
- TyrZ:
-
redox active tyrosine residue 161 of D1 protein
- WOC:
-
water-oxidizing complex
- ΔF:
-
photoinduced changes of chlorophyll fluorescence yield of PSII
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Acknowledgements: The work was supported by the Russian Science Foundation (grant 14-14-00535). We thank T. Smolova for isolation, purification of PsbO protein from pea chloroplast and I. Proskuryakov for EPR measurements.
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Khorobrykh, A.A., Yanykin, D.V. & Klimov, V.V. Photooxidation and photoreduction of exogenous cytochrome c by photosystem II preparations after various modifications of the water-oxidizing complex. Photosynthetica 56, 244–253 (2018). https://doi.org/10.1007/s11099-017-0762-8
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DOI: https://doi.org/10.1007/s11099-017-0762-8