On wavelength-dependent exciton lifetime distributions in reconstituted CP29 antenna of the photosystem II and its site-directed mutants

2021 ◽  
Vol 154 (8) ◽  
pp. 085101
Author(s):  
Tonu Reinot ◽  
Mahboobe Jassas ◽  
Adam Kell ◽  
Anna Paola Casazza ◽  
Stefano Santabarbara ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Lifetime Distributions ◽  
Exciton Lifetime

Characterization of photosystem II with the atomic-force microscope

1992 ◽  
Vol 50 (2) ◽  
pp. 1146-1147
Author(s):  
Kathleen M. Marr ◽  
Mary K. Lyon
Keyword(s):  
Photosystem Ii ◽  
Atomic Force Microscope ◽  
Three Dimensional ◽  
Biologically Active ◽  
Atomic Force ◽  
Freeze Etching ◽  
Image Averaging ◽  
Oxygen Evolving ◽  
Averaging Techniques

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.

Involvement of protein phosphorylation in the sensitivity of photosystem II to strong illumination

1994 ◽  
Vol 92 (1) ◽  
pp. 181-187
Author(s):  
Maria T. Giardi ◽  
Josef Komenda ◽  
Jiri Masojidek
Keyword(s):  
Photosystem Ii ◽  
Protein Phosphorylation
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