The Influence of Quinone Structure on Quinone Binding to the QA Site in Bacterial Reaction Centers from Rhodobacter Sphaeroides

1998 ◽  
pp. 877-880 ◽  
Author(s):  
Ralf Schmid ◽  
Andreas Labahn
Keyword(s):  
Rhodobacter Sphaeroides ◽  
Reaction Centers ◽  
Quinone Binding ◽  
Bacterial Reaction Centers ◽  
Quinone Structure

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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