The mutation of carotenoids affects the energy transfer in LH2 light harvesting complexes from Rhodobacter sphaeroides 601 at room temperature

2006 ◽  
Vol 119-120 ◽  
pp. 350-355 ◽  
Author(s):  
Weimin Liu ◽  
Yuan Liu ◽  
Lijun Guo ◽  
Chunhe Xu ◽  
Shixiong Qian
1993 ◽  
Vol 57 (1) ◽  
pp. 49-55 ◽  
Author(s):  
Harry A. Frank ◽  
Roya Farhoosh ◽  
Mila L. Aldema ◽  
Beverly DeCoster ◽  
Ronald L. Christensen ◽  
...  

1990 ◽  
Vol 87 (1) ◽  
pp. 215-219 ◽  
Author(s):  
J. K. Trautman ◽  
A. P. Shreve ◽  
C. A. Violette ◽  
H. A. Frank ◽  
T. G. Owens ◽  
...  

Science ◽  
2013 ◽  
Vol 340 (6139) ◽  
pp. 1448-1451 ◽  
Author(s):  
R. Hildner ◽  
D. Brinks ◽  
J. B. Nieder ◽  
R. J. Cogdell ◽  
N. F. van Hulst

Science ◽  
2018 ◽  
Vol 360 (6393) ◽  
pp. 1109-1113 ◽  
Author(s):  
Xiaowei Pan ◽  
Jun Ma ◽  
Xiaodong Su ◽  
Peng Cao ◽  
Wenrui Chang ◽  
...  

Plants regulate photosynthetic light harvesting to maintain balanced energy flux into photosystems I and II (PSI and PSII). Under light conditions favoring PSII excitation, the PSII antenna, light-harvesting complex II (LHCII), is phosphorylated and forms a supercomplex with PSI core and the PSI antenna, light-harvesting complex I (LHCI). Both LHCI and LHCII then transfer excitation energy to the PSI core. We report the structure of maize PSI-LHCI-LHCII solved by cryo–electron microscopy, revealing the recognition site between LHCII and PSI. The PSI subunits PsaN and PsaO are observed at the PSI-LHCI interface and the PSI-LHCII interface, respectively. Each subunit relays excitation to PSI core through a pair of chlorophyll molecules, thus revealing previously unseen paths for energy transfer between the antennas and the PSI core.


1996 ◽  
Vol 259 (3-4) ◽  
pp. 381-390 ◽  
Author(s):  
Marilena Ricci ◽  
Stephen E. Bradforth ◽  
Ralph Jimenez ◽  
Graham R. Fleming

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