Circadian expression of the light-harvesting protein of Photosystem II in etiolated bean leaves following a single red light pulse: Coordination with the capacity of the plant to form chlorophyll and the thylakoid-bound protease

1995 ◽  
Vol 44 (1-2) ◽  
pp. 93-106 ◽  
Author(s):  
T. Bei-Paraskevopoulou ◽  
R. Anastassiou ◽  
J. Argyroudi-Akoyunoglou
2021 ◽  
Author(s):  
Makiko Kosugi ◽  
Masato Kawasaki ◽  
Yutaka Shibata ◽  
Kojiro Hara ◽  
Shinichi Takaichi ◽  
...  

Abstract Prasiola crispa, a major green alga in Antarctica, forms layered colonies for survival under the severe terrestrial conditions of Antarctica, which include severe cold, drought, and strong sunlight. As a result of these conditions, the surface cells of P. crispa and other Antarctic organisms face high risk of photodamage. Cells of deeper layer escape from photodamage at the sacrifice of photosynthetic active radiation except infrared. P. crispa achieves effective photosynthesis by low energy far-red light for photosystem II excitation with high efficiency similar to that of visible light. Here, we identified a far-red light-harvesting complex of photosystem II in P. crispa, Pc-frLHC, and proposed a molecular mechanism of uphill excitation energy transfer based on its cryogenic electron-microscopy structure. While Pc-frLHC is associated with photosystem II, it is evolutionarily related to the light-harvesting complex of photosystem I. Pc-frLHC forms a ring-shaped homo-undecamer in which all chlorophyll a molecules are energetically connected and contains chlorophyll a trimers. It seems that the trimers are long-wavelength-absorbing chlorophylls for far-red light at 708 nm, and further absorbance extension is accomplished by Davydov-splitting in dimeric chlorophylls. The chlorophyll network should enable a highly efficient entropy-driven uphill excitation energy transfer using far-red light up to 725 nm.


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.


2021 ◽  
Vol 258 ◽  
pp. 123932
Author(s):  
Lekha Peedikakkandy ◽  
Ondřej Pavelka ◽  
Martina Alsterová ◽  
Anna Fučíková ◽  
Jakub Dostál ◽  
...  

Biochemistry ◽  
1998 ◽  
Vol 37 (33) ◽  
pp. 11586-11591 ◽  
Author(s):  
Alexander V. Ruban ◽  
Paolo Pesaresi ◽  
Ulrich Wacker ◽  
Klaus-Dieter J. Irrgang ◽  
Roberto Bassi ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document