scholarly journals Time-resolved fluorescence study of excitation energy transfer in the cyanobacterium Anabaena PCC 7120

2020 ◽  
Vol 144 (2) ◽  
pp. 247-259 ◽  
Author(s):  
Parveen Akhtar ◽  
Avratanu Biswas ◽  
Nia Petrova ◽  
Tomas Zakar ◽  
Ivo H. M. van Stokkum ◽  
...  
Keyword(s):  
Energy Transfer ◽  
Excitation Energy ◽  
Excitation Energy Transfer ◽  
Time Resolved Fluorescence ◽  
Fluorescence Study ◽  
Time Resolved ◽  
Anabaena Pcc 7120 ◽  
Cyanobacterium Anabaena ◽  
Pcc 7120

scholarly journals Modelling excitation energy transfer and trapping in the filamentous cyanobacterium Anabaena variabilis PCC 7120

2020 ◽  
Vol 144 (2) ◽  
pp. 261-272 ◽  
Author(s):  
Avratanu Biswas ◽  
Xinpeng Huang ◽  
Petar H. Lambrev ◽  
Ivo H. M. van Stokkum
Keyword(s):  
Energy Transfer ◽  
Excitation Energy ◽  
Excitation Energy Transfer ◽  
Anabaena Variabilis ◽  
Filamentous Cyanobacterium ◽  
Cyanobacterium Anabaena ◽  
Pcc 7120

scholarly journals Structure of a cyanobacterial photosystem I tetramer revealed by cryo-electron microscopy

2019 ◽  
Vol 10 (1) ◽  
Author(s):  
Koji Kato ◽  
Ryo Nagao ◽  
Tian-Yi Jiang ◽  
Yoshifumi Ueno ◽  
Makio Yokono ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Excitation Energy ◽  
Photosystem I ◽  
Excitation Energy Transfer ◽  
Time Resolved Fluorescence ◽  
Time Resolved ◽  
Dimer Interface ◽  
Cryo Electron Microscopy ◽  
Evolutionary Changes ◽  
Pcc 7120

Abstract Photosystem I (PSI) functions to harvest light energy for conversion into chemical energy. The organisation of PSI is variable depending on the species of organism. Here we report the structure of a tetrameric PSI core isolated from a cyanobacterium, Anabaena sp. PCC 7120, analysed by single-particle cryo-electron microscopy (cryo-EM) at 3.3 Å resolution. The PSI tetramer has a C2 symmetry and is organised in a dimer of dimers form. The structure reveals interactions at the dimer-dimer interface and the existence of characteristic pigment orientations and inter-pigment distances within the dimer units that are important for unique excitation energy transfer. In particular, characteristic residues of PsaL are identified to be responsible for the formation of the tetramer. Time-resolved fluorescence analyses showed that the PSI tetramer has an enhanced excitation-energy quenching. These structural and spectroscopic findings provide insights into the physiological significance of the PSI tetramer and evolutionary changes of the PSI organisations.

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