Conformational Changes Induced by Phosphorylation in the CP29 Subunit of Photosystem II†,‡

Biochemistry ◽  
1996 ◽  
Vol 35 (34) ◽  
pp. 11142-11148 ◽  
Author(s):  
Roberta Croce ◽  
Jacques Breton ◽  
Roberto Bassi
Keyword(s):  
Photosystem Ii ◽  
Conformational Changes

Conformational changes of the intermediate of the S2 to S3 transition in photosystem II

2011 ◽  
Vol 104 (1-2) ◽  
pp. 72-79 ◽  
Author(s):  
Maria Chrysina ◽  
Georgia Zahariou ◽  
Yiannis Sanakis ◽  
Nikolaos Ioannidis ◽  
Vasili Petrouleas
Keyword(s):  
Photosystem Ii ◽  
Conformational Changes

scholarly journals How to build a water-splitting machine: structural insights into photosystem II assembly

2020 ◽  
Author(s):  
Jure Zabret ◽  
Stefan Bohn ◽  
Sandra Schuller ◽  
Oliver Arnolds ◽  
Madeline Möller ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Water Splitting ◽  
Conformational Changes ◽  
Binding Pocket ◽  
Heme Iron ◽  
Structural Motif ◽  
Acceptor Side ◽  
Non Heme Iron ◽  
Assembly Intermediate ◽  
Stepwise Assembly

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.

Low pH-induced conformational changes in 33 kD protein of photosystem II

2004 ◽  
Vol 49 (9) ◽  
pp. 921-925
Author(s):  
Jun Weng ◽  
Cuiyan Tan ◽  
Yong Yu ◽  
Kangcheng Ruan ◽  
Chunhe Xu
Keyword(s):  
Photosystem Ii ◽  
Conformational Changes ◽  
Low Ph

scholarly journals Conformational Changes in Photosystem II Supercomplexes upon Removal of Extrinsic Subunits†

Biochemistry ◽  
2000 ◽  
Vol 39 (42) ◽  
pp. 12907-12915 ◽  
Author(s):  
Egbert J. Boekema ◽  
Jan F. L. van Breemen ◽  
Henny van Roon ◽  
Jan P. Dekker
Keyword(s):  
Photosystem Ii ◽  
Conformational Changes

Conformational Changes in the Extrinsic Manganese Stabilizing Protein Can Occur upon Binding to the Photosystem II Reaction Center:  An Isotope Editing and FT-IR Study†

Biochemistry ◽  
1998 ◽  
Vol 37 (16) ◽  
pp. 5643-5653 ◽  
Author(s):  
Ronald S. Hutchison ◽  
Scott D. Betts ◽  
Charles F. Yocum ◽  
Bridgette A. Barry
Keyword(s):  
Photosystem Ii ◽  
Reaction Center ◽  
Conformational Changes ◽  
Manganese Stabilizing Protein ◽  
Ft Ir ◽  
Ir Study

scholarly journals How to build a water-splitting machine: structural insights into photosystem II assembly

2020 ◽  
Author(s):  
Jure Zabret ◽  
Stefan Bohn ◽  
Sandra K. Schuller ◽  
Oliver Arnolds ◽  
Madeline Möller ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Water Splitting ◽  
Conformational Changes ◽  
Binding Pocket ◽  
Heme Iron ◽  
Structural Motif ◽  
Acceptor Side ◽  
Assembly Factors ◽  
Assembly Intermediate ◽  
Stepwise Assembly

AbstractBiogenesis 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.One Sentence HighlightThe high-resolution Cryo-EM structure of the photosystem II assembly intermediate PSII-I reveals how nature’s water splitting catalyst is assembled, protected and prepared for photoactivation by help of the three assembly factors Psb27, Psb28 and Psb34.

scholarly journals Femtosecond Nanocrystallography and Characterization of Photosystem II

2014 ◽  
Vol 70 (a1) ◽  
pp. C1141-C1141
Author(s):  
Christopher Kupitz ◽  
Shibom Basu ◽  
Ingo Grotjohann ◽  
Raimund Fromme ◽  
Dingjie Wang ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Photosystem Ii ◽  
Conformational Changes ◽  
Perfect Crystal ◽  
Diffusion Method ◽  
Time Resolved ◽  
X Ray Crystallography ◽  
Complex Membrane ◽  
Nonlinear Imaging ◽  
Chiral Crystals

Membrane proteins are extremely difficult to crystallize, however they are highly important proteins for cellular function. Photosystem I, one of the most complex membrane proteins solved to date took more than a decade to have a structure solved to molecular resolution. Large, well-ordered crystal growth is one of the major bottlenecks in structural determination by x-ray crystallography, due to the difficulty of making the "perfect" crystal. The development of femtosecond nanocrystallography, which uses a stream of fully hydrated nanocrystals to collect diffraction snapshots, effectively reduces this bottleneck[1] Photosystem II changed our biosphere via splitting water and evolving oxygen 2.5 billion years ago. Using femtosecond nanocrystallography we are developing a time-resolved femtosecond crystallography method [2] to unravel the mechanism of water splitting by determining the conformational changes that take place during the oxygen evolution process. Multiple crystallization techniques were originally developed in order to make the nanocrystals necessary for femtosecond nanocrystallography. For Photosystem II nano/microcrystals a free interface diffusion method, is used to increase yield over traditional methods. These crystals are then characterized by three different methods before being used for collecting diff raction data. The three methods currently used are optical microscopy, dynamic light scattering (DLS), and Second Order Nonlinear Imaging of Chiral Crystals (SONICC).

The study of conformational changes in photosystem II during a charge separation

2020 ◽  
Vol 26 (4) ◽  
Author(s):  
Natalia Kulik ◽  
Michal Kutý ◽  
David Řeha
Keyword(s):  
Photosystem Ii ◽  
Conformational Changes ◽  
Charge Separation ◽  
A Charge

Effects of aging on chlorophyll fluorescence and photosystem II electron transport in isolated chloroplasts

1975 ◽  
Vol 53 (23) ◽  
pp. 2842-2845 ◽  
Author(s):  
M. Fragata
Keyword(s):  
Fatty Acids ◽  
Chlorophyll Fluorescence ◽  
Photosystem Ii ◽  
Conformational Changes ◽  
Photochemical Activity ◽  
Photosynthetic Membrane ◽  
Fluorescence Characteristics ◽  
Protein Molecules ◽  
Effects Of Aging ◽  
Isolated Chloroplasts

The correlation between emission of energy and photochemical activity in isolated chloroplasts during aging was investigated. It was shown that aging hinders the intensity of chlorophyll-a fluorescence with a concomitant decrease of the photosystem II activity. In view of the parallelism between the action of exogenous fatty acids, especially C18-unsaturated acids, and the effects of aging, it is suggested that the thylakoid transformation during aging could result partly from conformational changes of the membrane polypeptides due to the presence of free fatty acids in the neighborhood of the protein molecules. It is possible that such a mechanism of fatty acid action may alter the fluorescence characteristics of chlorophyll as well as the tunneling of electrons in the photosynthetic membrane.

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