Uncoupling of detectable O2 evolution from the apparent S-state transitions in Photosystem II by lauroylcholine chloride: Possible implications in the photosynthetic water-splitting mechanism

1985 ◽  
Vol 809 (1) ◽  
pp. 125-136 ◽  
Author(s):  
T. Wydrzynski ◽  
B.J. Huggins ◽  
P.A. Jursinic
2018 ◽  
Vol 1859 (10) ◽  
pp. 1059-1066 ◽  
Author(s):  
Reza Ranjbar Choubeh ◽  
Emilie Wientjes ◽  
Paul C. Struik ◽  
Diana Kirilovsky ◽  
Herbert van Amerongen

2015 ◽  
Vol 112 (5) ◽  
pp. 1613-1618 ◽  
Author(s):  
Xin Hou ◽  
Aigen Fu ◽  
Veder J. Garcia ◽  
Bob B. Buchanan ◽  
Sheng Luan

In earlier studies we have identified FKBP20-2 and CYP38 as soluble proteins of the chloroplast thylakoid lumen that are required for the formation of photosystem II supercomplexes (PSII SCs). Subsequent work has identified another potential candidate functional in SC formation (PSB27). We have followed up on this possibility and isolated mutants defective in the PSB27 gene. In addition to lack of PSII SCs, mutant plants were severely stunted when cultivated with light of variable intensity. The stunted growth was associated with lower PSII efficiency and defective starch accumulation. In response to high light exposure, the mutant plants also displayed enhanced ROS production, leading to decreased biosynthesis of anthocyanin. Unexpectedly, we detected a second defect in the mutant, namely in CP26, an antenna protein known to be required for the formation of PSII SCs that has been linked to state transitions. Lack of PSII SCs was found to be independent of PSB27, but was due to a mutation in the previously described cp26 gene that we found had no effect on light adaptation. The present results suggest that PSII SCs, despite being required for state transitions, are not associated with acclimation to changing light intensity. Our results are consistent with the conclusion that PSB27 plays an essential role in enabling plants to adapt to fluctuating light intensity through a mechanism distinct from photosystem II supercomplexes and state transitions.


2018 ◽  
Vol 8 (4) ◽  
Author(s):  
Katherine M. Davis ◽  
Brendan T. Sullivan ◽  
Mark C. Palenik ◽  
Lifen Yan ◽  
Vatsal Purohit ◽  
...  

2008 ◽  
Vol 27 (5) ◽  
pp. 782-791 ◽  
Author(s):  
Tatiana Shutova ◽  
Hella Kenneweg ◽  
Joachim Buchta ◽  
Julia Nikitina ◽  
Vasily Terentyev ◽  
...  

2016 ◽  
Vol 39 (7) ◽  
pp. 1524-1536 ◽  
Author(s):  
Dmitriy Shevela ◽  
Janine Arnold ◽  
Veronika Reisinger ◽  
Hans-Martin Berends ◽  
Karol Kmiec ◽  
...  

2020 ◽  
Author(s):  
Jure Zabret ◽  
Stefan Bohn ◽  
Sandra Schuller ◽  
Oliver Arnolds ◽  
Madeline Möller ◽  
...  

Abstract Biogenesis of photosystem II (PSII), nature’s water splitting catalyst, is assisted by auxiliary proteins that form transient complexes with PSII components to facilitate stepwise assembly events. Using cryo-electron microscopy, we solved the structure of such a PSII assembly intermediate with 2.94 Å resolution. It contains three assembly factors (Psb27, Psb28, Psb34) and provides detailed insights into their molecular function. Binding of Psb28 induces large conformational changes at the PSII acceptor side, which distort the binding pocket of the mobile quinone (QB) and replace bicarbonate with glutamate as a ligand of the non-heme iron, a structural motif found in reaction centers of non-oxygenic photosynthetic bacteria. These results reveal novel mechanisms that protect PSII from damage during biogenesis until water splitting is activated. Our structure further demonstrates how the PSII active site is prepared for the incorporation of the Mn4CaO5 cluster, which performs the unique water splitting reaction.


2014 ◽  
Vol 106 (2) ◽  
pp. 27a
Author(s):  
Yulia Pushkar ◽  
Katherine Davis ◽  
Lifen Yan

2021 ◽  
pp. 3-38
Author(s):  
Jian-Ren Shen ◽  
Yoshiki Nakajima ◽  
Fusamichi Akita ◽  
Michihiro Suga

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