Phthalocyanine as a Bioinspired Model for Chlorophyll f ‐Containing Photosystem II Drives Photosynthesis into the Far‐Red Region

Author(s):  
Jorge Follana‐Berná ◽  
Rajaa Farran ◽  
Winfried Leibl ◽  
Annamaria Quaranta ◽  
Ángela Sastre‐Santos ◽  
...  
Keyword(s):  
2021 ◽  
Author(s):  
Jorge Follana‐Berná ◽  
Rajaa Farran ◽  
Winfried Leibl ◽  
Annamaria Quaranta ◽  
Ángela Sastre‐Santos ◽  
...  
Keyword(s):  

Nature Plants ◽  
2020 ◽  
Vol 6 (3) ◽  
pp. 238-244 ◽  
Author(s):  
Joko P. Trinugroho ◽  
Martina Bečková ◽  
Shengxi Shao ◽  
Jianfeng Yu ◽  
Ziyu Zhao ◽  
...  
Keyword(s):  

Nature Plants ◽  
2020 ◽  
Vol 6 (4) ◽  
pp. 427-427
Author(s):  
Joko P. Trinugroho ◽  
Martina Bečková ◽  
Shengxi Shao ◽  
Jianfeng Yu ◽  
Ziyu Zhao ◽  
...  
Keyword(s):  

Author(s):  
Jorge Follana‐Berná ◽  
Rajaa Farran ◽  
Winfried Leibl ◽  
Annamaria Quaranta ◽  
Ángela Sastre‐Santos ◽  
...  
Keyword(s):  

2021 ◽  
Author(s):  
Jorge Follana‐Berná ◽  
Rajaa Farran ◽  
Winfried Leibl ◽  
Annamaria Quaranta ◽  
Ángela Sastre‐Santos ◽  
...  
Keyword(s):  

2021 ◽  
Author(s):  
Vincenzo Mascoli ◽  
Ahmad Farhan Bhatti ◽  
Luca Bersanini ◽  
Herbert van Amerongen ◽  
Roberta Croce

Cyanobacteria carry out photosynthetic light-energy conversion using phycobiliproteins for light harvesting and the chlorophyll-rich photosystems for photochemistry. While most cyanobacteria only absorb visible photons, some of them can acclimate to harvest far-red light (FRL, 700-800 nm) by integrating chlorophyll f and d in their photosystems and producing red-shifted allophycocyanin. Chlorophyll f insertion enables the photosystems to use FRL but slows down charge separation, reducing photosynthetic efficiency. Here we demonstrate with time-resolved fluorescence spectroscopy that charge separation in chlorophyll-f-containing Photosystem II becomes faster in the presence of red-shifted allophycocyanin antennas. This is different from all known photosynthetic systems, where additional light-harvesting complexes slow down charge separation. Based on the available structural information, we propose a model for the connectivity between the phycobiliproteins and Photosystem II that qualitatively accounts for our spectroscopic data. This unique design is probably important for these cyanobacteria to efficiently switch between visible and far-red light.


Science ◽  
2016 ◽  
Vol 353 (6302) ◽  
pp. aaf9178-aaf9178 ◽  
Author(s):  
M.-Y. Ho ◽  
G. Shen ◽  
D. P. Canniffe ◽  
C. Zhao ◽  
D. A. Bryant
Keyword(s):  

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.


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