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1993 (1)
1991 (1)
1990 (1)
1Author    G. Á Bor Horváth, M. Agdolna, D. Roppa, Ágnes PuskáRequires cookie*
 Title    Fluorescence Induction Characteristics of Wild-Type and Herbicide-Resistant Strain of the Photosynthetic Bacterium Rhodobacter capsulatus  
 Abstract    Fluorescence induction characteristics have been studied in wild-type and atrazine-resistant mutant o f Rhodobacter capsulatus. Fluorescence induction was found to be a useful technique to monitor the altered electron transfer in the atrazine-resistant mutants as well as in the differ­ ent membrane fractions o f wild-type R. capsulatus. In both cases, the proportion o f the fast rise o f variable fluorescence was increased indicating the enhancement o f QA. In the mutant strain, the / 50 value o f triazine herbicide terbutryn was increased by 1 0 0 -fold whereas the natu­ ral resistance o f R . capsulatus against diuron was abolished by the mutation. 
  Reference    Z. Naturforsch. 45c, 452 (1990); received N ovem ber 9 1989 
  Published    1990 
  Keywords    Fluorescence Induction, Electron Transport, Herbicide, Purple Bacteria, Photosynthesis 
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 TEI-XML for    default:Reihe_C/45/ZNC-1990-45c-0452.pdf 
 Identifier    ZNC-1990-45c-0452 
 Volume    45 
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 
3Author    J.-H KlemmeRequires cookie*
 Title    Photoproduction of Hydrogen by Purple Bacteria: A Critical Evaluation of the Rate Limiting Enzymatic Steps  
 Abstract    The enzymatic mechanisms and energetics o f nitrogenase-catalyzed photoproduction o f hydrogen from organic C -com pounds by purple bacteria are discussed in respect to the ques­ 
  Reference    Z. Naturforsch. 48c, 482 (1993); received January 15 1993 
  Published    1993 
  Keywords    Hydrogen, Hydrogenase, N itrogenase, Purple Bacteria, Photosynthesis 
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 TEI-XML for    default:Reihe_C/48/ZNC-1993-48c-0482.pdf 
 Identifier    ZNC-1993-48c-0482 
 Volume    48