Go toArchive
Browse byFacets
Bookbag ( 0 )
'A llosteric interaction' in keywords Facet   section ZfN Section C  [X]
Results  1 Item
Sorted by   
Publication Year
1984 (1)
1Author    W. Im, F. J. Vermaas, G. Ern O, R. Enger, J. A. Arles, RntzenRequires cookie*
 Title    Herbicide/Quinone Binding Interactions in Photosystem II  
 Abstract    Many inhibitors prevent the oxidation o f the primary electron-accepting quinone (Q A) by the secondary quinone (Q B) in photosystem II by displacem ent o f Q B from its binding site. On the other hand, plastoquinone-1 and 6-azido-5-decyl-2,3-dim ethoxy-/?-benzoquinone displace herbicides. Binding studies show the herbicide/quinone interaction to be (apparently) competitive. The herbicide binding is influenced differentially by various treatments. In this paper it is shown that the affinity of, for example, brom oxynil is decreased by thylakoid unstacking or by light-or reductant-induced reduction o f certain thylakoid com ponents, whereas atrazine affinity remains unchanged. Furthermore, absence o f H C O j in the presence o f form ate leads to an affinity decrease o f bromoxynil and atrazine, but to an increase in i-dinoseb affinity. Other differential photosystem II herbicide effects are known from the literature. Since different and unrelated groups o f Q A oxidation inhibitors have been found, and because o f the above-mentioned dissim ilarities in binding characteristics for different inhibitor groups, the hypothesis o f non-identical, but "overlapping" binding sites for different herbicide groups and the native quinone must be more extensively defined. In this m anuscript we evaluate both the competitive herbicide/quinone binding m odel, and a m odel in which binding o f one ligand alters the protein conformation resulting in a dram atic decrease in the binding affinity o f ligands from other chemical groups; in this model ligands from the sam e or related chem ical groups bind competitively. Thus, the latter model proposes that only one herbicide or quinone m olecule can be bound with high affinity to the herbicide/quinone binding environm ent, but it depends on the chemical structure o f the ligands whether the binding interaction betw een two ligands is truly competitive or more indirect (allosteric), m ediated through the protein conform ation. 
  Reference    Z. Naturforsch. 39c, 368 (1984); received D ecem ber 1 1983 
  Published    1984 
  Keywords    Herbicide, Photosystem II, Plastoquinone, Photosynthesis, A llosteric interaction 
  Similar Items    Find
 DEBUG INFO      
 TEI-XML for    default:Reihe_C/39/ZNC-1984-39c-0368.pdf 
 Identifier    ZNC-1984-39c-0368 
 Volume    39