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'Quinones' in keywords Facet   Publication Year 1991  [X]
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1991[X]
1Author    DaivaA. Bironaitė, N. Arim, K. Čėnas, JuozasJ. Kulys, AlexanderG. Medentsev, VasiliyK. Akimenko, P. A. Karplus, E. F. Pai, G. E. Schulz, EurJ. BiochemRequires cookie*
 Title      
 Abstract    Fully substituted quinones including som e naturally occurring oxyquinones acted as inhibitors o f yeast gluta­ thione reductase (EC 1.6.4.2). They were competitive, mixed or uncompetitive inhibitors for N A D P H , possess­ ing K j in the range o f 1 -2 0 0 |iM and uncompetitive in­ hibitors for glutathione. Rhein (4,5-dioxy-9,10-anthra-quinone-2-carbonic acid) and 9,10-phenanthrenequi-none were the most effective inhibitors. It is concluded that certain quinones can bind to the N A D P(H)-binding site and to the heteroaromatics binding site at the inter­ face domain (o f the enzyme. 
  Reference    Z. Naturforsch. 46c, 966—9 (1991); received March 4/M ay 71991. 178 6 9 3 -7 0 3 1989 
  Published    1991 
  Keywords    Glutathione Reductase, Inhibition, Quinones 
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 TEI-XML for    default:Reihe_C/46/ZNC-1991-46c-0966_n.pdf 
 Identifier    ZNC-1991-46c-0966_n 
 Volume    46 
2Author    I. Agalidis, E. Rivasb, F. Reiss-HussonaRequires cookie*
 Title    Characterization of Reaction Center-B875 Complex of Rhodocyclus gelatinosus: Q B Site Properties Derived from Reconstitution Experiments  
 Abstract    Purified reaction center-B875 pigment-protein complex isolated from Rc. gelatinosus (I. Agalidis, E. Rivas, and F. Reiss-Husson, Photosynth. Res. 23, 2 4 9 -2 5 5 (1990)) was further characterized. In the chromatophores, the quinone content was shown to be 6 menaquinones 8 and 16 ubiquinones 8 per reaction center, indicating that the pool contained both quinone types. Besides the primary (M K S) and secondary (U Q X) electron acceptors o f the reaction cen­ ter, the com plex contains residual quinones from the membrane pool (about 3 M K X and 5 U Q 8) probably associated with the phospholipids. Apparent particle weight o f the complex including bound detergent was 520 ± 46 kDa. The secondary quinone Q B was partially removed from the RC by treatment with 2 -3 % octaethyleneglycol dodecyl ether and 3 —4 m M orthophenanthroline. Reconstitution experi­ ments showed that U Q 6, U Q 9 and U Q ,0 could replace Q B but that M K S and M K , could not. It was concluded that Q B site has a clear specificity towards ubiquinone binding. 
  Reference    Z. Naturforsch. 46c, 99—105 (1991); received October 10/November 26 1990 
  Published    1991 
  Keywords    Purple Bacteria, Reaction Center, Secondary Electron Acceptor, Quinones 
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 TEI-XML for    default:Reihe_C/46/ZNC-1991-46c-0099.pdf 
 Identifier    ZNC-1991-46c-0099 
 Volume    46