Binding sites of lipophilic quinone and quinone analogue inhibitors in the cytochrome b6f complex of oxygenic photosynthesis

2005 ◽  
Vol 33 (5) ◽  
pp. 921
Author(s):  
H. Zhang ◽  
W.A. Cramer ◽  
J. Yan ◽  
G. Kurisu
2005 ◽  
Vol 33 (5) ◽  
pp. 921-923 ◽  
Author(s):  
W.A. Cramer ◽  
H. Zhang ◽  
J. Yan ◽  
G. Kurisu

The main structural features of the cytochrome b6f complex, solved to 3.0–3.1 Å (1 Å=10−10 m) in the cyanobacterium Mastigocladus laminosus and the green alga Chlamydomonas reinhardtii are discussed. The discussion is focused on the binding sites of plastoquinone and quinone analogue inhibitors discerned in the structure. These sites mark the pathway(s) of quinone translocation across the complex.


2013 ◽  
Vol 104 (2) ◽  
pp. 488a
Author(s):  
Stanislav D. Zakharov ◽  
Syed Saif Hasan ◽  
Adrien Chauvet ◽  
Sergei Savikhin ◽  
William A. Cramer

2016 ◽  
Vol 18 (18) ◽  
pp. 12983-12991 ◽  
Author(s):  
Adrien A. P. Chauvet ◽  
Rachna Agarwal ◽  
André al Haddad ◽  
Frank van Mourik ◽  
William A. Cramer

The ultrafast behavior of the ferrous heme f from the cytochrome b6f complex of oxygenic photosynthesis is revealed by means of transient absorption spectroscopy.


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