Regulation of the Primary Quinone Binding Conformation by the H Subunit in Reaction Centers from Rhodobacter sphaeroides

2015 ◽  
Vol 6 (22) ◽  
pp. 4541-4546 ◽  
Author(s):  
Chang Sun ◽  
Alexander T. Taguchi ◽  
Nathan J. Beal ◽  
Patrick J. O’Malley ◽  
Sergei A. Dikanov ◽  
...  
Keyword(s):  
Rhodobacter Sphaeroides ◽  
Reaction Centers ◽  
Quinone Binding ◽  
Binding Conformation

The IleL229 ? Met mutation impairs the quinone binding to the QB-pocket in reaction centers of Rhodobacter sphaeroides

1995 ◽  
Vol 45 (2) ◽  
pp. 135-146 ◽  
Author(s):  
J�lia Tandori ◽  
L�szl� Nagy ◽  
�gnes Pusk�s ◽  
Magdolna Droppa ◽  
G�bor Horv�th ◽  
...  
Keyword(s):  
Rhodobacter Sphaeroides ◽  
Reaction Centers ◽  
Quinone Binding

Herbicide and Quinone Binding to Chromatophores and Reaction Centers from Rhodobacter sphaeroides

1987 ◽  
Vol 42 (6) ◽  
pp. 690-692 ◽  
Author(s):  
Walter Oettmeier ◽  
Silvana Preuße
Keyword(s):  
Cytochrome C ◽  
Rhodobacter Sphaeroides ◽  
Higher Plants ◽  
Electron Flow ◽  
Reaction Centers ◽  
Type Reaction ◽  
Photosynthetic Electron Flow ◽  
Quinone Binding ◽  
Bacterial Reaction Centers

Besides s-triazine and triazinone herbicides the chromone stigmatellin and tetrahalogen-substituted 1.4-benzoquinones are inhibitors of photosynthetic electron flow from reduced cytochrome c to ubiquinone-6 in isolated bacterial reaction centers. With isolated bacterial chromatophores binding experiments with radiolabeled herbicides can be performed in a similar way as with thylakoids from higher plants. Tetrahalogen-substituted 1.4-benzoquinones in a Michael type reaction can add onto nucleophilic groups in proteins. In bacterial reaction centers, a [14C]tetra- bromo-1.4-benzoquinone (bromanil) exclusively binds to the H-subunit.

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