Sensitivity of Photosystems II to NaCl in Relation to Salinity Tolerance. Comparative Studies With Thylakoids of the Salt Tolerant Mangrove, Avicennia marina, and the Salt-Sensitive Pea, Pisum sativum

1986 ◽  
Vol 13 (5) ◽  
pp. 689 ◽  
Author(s):  
MC Ball ◽  
JM Anderson

The sensitivity of photosystem II to NaCl was compared in thylakoids isolated from the salt-tolerant mangrove, Avicennia marina, and the salt-sensitive pea, Pisum sativum. There were no indications of fundamental differences in photosystem II between these two species. Rates of oxygen evolution declined linearly with increase in NaCl from 10 to 500 mol m-3, with both species being equally sensitive. The NaCl-induced changes in Chl a fluorescence characteristics of intact thylakoids were substantially reversed by addition of hydroxylamine, indicating that the water-oxidizing site of photosystem II is sensitive to the NaCl concentration. These results are consistent with NaCl-induced depletion of the 23 and 17 kDa proteins from photosystem II-enriched membrane sheets. While the inhibition of oxygen-evolving activity by 500 mol m-3 NaCl was substantially reversed in thylakoids kept in the dark, 500 mol m-3 NaCl induced marked photoinhibitory damage in illuminated thylakoids. Thus, accumulation of ions in the chloroplasts of either salt-tolerant or salt-sensitive species would probably result in rapid damage to photosystem II, particularly in the light.




Science ◽  
2019 ◽  
Vol 365 (6452) ◽  
pp. eaax4406 ◽  
Author(s):  
Xiong Pi ◽  
Songhao Zhao ◽  
Wenda Wang ◽  
Desheng Liu ◽  
Caizhe Xu ◽  
...  

Diatoms play important roles in global primary productivity and biogeochemical cycling of carbon, in part owing to the ability of their photosynthetic apparatus to adapt to rapidly changing light intensity. We report a cryo–electron microscopy structure of the photosystem II (PSII)–fucoxanthin (Fx) chlorophyll (Chl) a/c binding protein (FCPII) supercomplex from the centric diatom Chaetoceros gracilis. The supercomplex comprises two protomers, each with two tetrameric and three monomeric FCPIIs around a PSII core that contains five extrinsic oxygen-evolving proteins at the lumenal surface. The structure reveals the arrangement of a huge pigment network that contributes to efficient light energy harvesting, transfer, and dissipation processes in the diatoms.



Author(s):  
Kathleen M. Marr ◽  
Mary K. Lyon

Photosystem II (PSII) is different from all other reaction centers in that it splits water to evolve oxygen and hydrogen ions. This unique ability to evolve oxygen is partly due to three oxygen evolving polypeptides (OEPs) associated with the PSII complex. Freeze etching on grana derived insideout membranes revealed that the OEPs contribute to the observed tetrameric nature of the PSIl particle; when the OEPs are removed, a distinct dimer emerges. Thus, the surface of the PSII complex changes dramatically upon removal of these polypeptides. The atomic force microscope (AFM) is ideal for examining surface topography. The instrument provides a topographical view of individual PSII complexes, giving relatively high resolution three-dimensional information without image averaging techniques. In addition, the use of a fluid cell allows a biologically active sample to be maintained under fully hydrated and physiologically buffered conditions. The OEPs associated with PSII may be sequentially removed, thereby changing the surface of the complex by one polypeptide at a time.



Biomolecules ◽  
2019 ◽  
Vol 9 (8) ◽  
pp. 371
Author(s):  
Koua

The Mn4CaO5 cluster site in the oxygen-evolving complex (OEC) of photosystem II (PSII) undergoes structural perturbations, such as those induced by Ca2+/Sr2+ exchanges or Ca/Mn removal. These changes have been known to induce long-range positive shifts (between +30 and +150 mV) in the redox potential of the primary quinone electron acceptor plastoquinone A (QA), which is located 40 Å from the OEC. To further investigate these effects, we reanalyzed the crystal structure of Sr-PSII resolved at 2.1 Å and compared it with the native Ca-PSII resolved at 1.9 Å. Here, we focus on the acceptor site and report the possible long-range interactions between the donor, Mn4Ca(Sr)O5 cluster, and acceptor sites.



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