Study of the Carotenoid Binding Pocket of the Photosynthetic Reaction Centre from the Purple Bacterium Rhodobacter Sphaeroides

Author(s):  
P. Fyfe ◽  
R. J. Cogdell ◽  
C. N. Hunter ◽  
M. R. Jones
2005 ◽  
Vol 33 (4) ◽  
pp. 845-850 ◽  
Author(s):  
A.Y. Mulkidjanian ◽  
M.A. Kozlova ◽  
D.A. Cherepanov

This review is focused on reactions that gate (control) the electron transfer between the primary quinone QA and secondary quinone QB in the photosynthetic reaction centre of Rhodobacter sphaeroides. The results on electron and proton transfer are discussed in relation to structural information and to the steered molecular dynamics simulations of the QB ring flip in its binding pocket. Depending on the initial position of QB in the pocket and on certain conditions, the rate of electron transfer is suggested to be limited either by the quinone ring flip or by the charge-compensating proton equilibration between the surface and the buried QB site.


1998 ◽  
Vol 26 (3) ◽  
pp. S209-S209
Author(s):  
Justin P. Ridge ◽  
Matthew G. Goodwin ◽  
Marion van Brederode ◽  
Rienk van Grondelle ◽  
Michael R. Jones

1989 ◽  
Vol 9 (6) ◽  
pp. 763-763
Author(s):  
J. Deisenhofer ◽  
H. Michel

FEBS Letters ◽  
2000 ◽  
Vol 472 (1) ◽  
pp. 114-116 ◽  
Author(s):  
Andreas Kuglstatter ◽  
Jaroslava Miksovska ◽  
Pierre Sebban ◽  
Günter Fritzsch

1989 ◽  
Vol 9 (4) ◽  
pp. 383-419 ◽  
Author(s):  
Johann Deisenhofer ◽  
Harmut Michel

We first describe the history and methods of membrane protein crystallization, and show how the structure of the photosynthetic reaction centre from the purple bacterium Rhodopseudomonas viridis was solved. The structure of this membrane protein complex is correlated with its function as a light-driven electron pump across the photosynthetic membrane. Finally we draw conclusions on the structure of the photosystem II reaction centre from plants and discuss the aspects of membrane protein structure.


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