Spectroscopic Characterization of the Excitation Energy Transfer in the Fucoxanthin–Chlorophyll Protein of Diatoms

2005 ◽  
Vol 86 (1-2) ◽  
pp. 241-250 ◽  
Author(s):  
Emmanouil Papagiannakis ◽  
Ivo H.M. van Stokkum ◽  
Holger Fey ◽  
Claudia Büchel ◽  
Rienk van Grondelle
1996 ◽  
Vol 260 (1-2) ◽  
pp. 147-152 ◽  
Author(s):  
Seiji Akimoto ◽  
Sinichi Takaichi ◽  
Takehiko Ogata ◽  
Yoshinobu Nishimura ◽  
Iwao Yamazaki ◽  
...  

FEBS Letters ◽  
1987 ◽  
Vol 225 (1-2) ◽  
pp. 59-66 ◽  
Author(s):  
Richard S. Williams ◽  
John F. Allen ◽  
Anthony P.R. Brain ◽  
R.John Ellis

2008 ◽  
Vol 112 (4) ◽  
pp. 1204-1212 ◽  
Author(s):  
Chao-Ping Hsu ◽  
Zhi-Qiang You ◽  
Hung-Cheng Chen

2021 ◽  
Vol 4 (1) ◽  
Author(s):  
Orkun Çoruh ◽  
Anna Frank ◽  
Hideaki Tanaka ◽  
Akihiro Kawamoto ◽  
Eithar El-Mohsnawy ◽  
...  

AbstractA high-resolution structure of trimeric cyanobacterial Photosystem I (PSI) from Thermosynechococcus elongatus was reported as the first atomic model of PSI almost 20 years ago. However, the monomeric PSI structure has not yet been reported despite long-standing interest in its structure and extensive spectroscopic characterization of the loss of red chlorophylls upon monomerization. Here, we describe the structure of monomeric PSI from Thermosynechococcus elongatus BP-1. Comparison with the trimer structure gave detailed insights into monomerization-induced changes in both the central trimerization domain and the peripheral regions of the complex. Monomerization-induced loss of red chlorophylls is assigned to a cluster of chlorophylls adjacent to PsaX. Based on our findings, we propose a role of PsaX in the stabilization of red chlorophylls and that lipids of the surrounding membrane present a major source of thermal energy for uphill excitation energy transfer from red chlorophylls to P700.


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