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'Synechococcus PCC 7942' in keywords
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1992 (1)
1990 (1)
1Author    Nir Ohad3, Dekel Amir-Shapirab, Hiroyuki Koikec, Yorinao Inouec, Itzhak Ohadb, Joseph Hirschberg3Requires cookie*
 Title    Amino Acid Substitutions in the D 1 Protein of Photosystem II Affect Q b-Stabilization and Accelerate Turnover of D  
 Abstract    Isogenic strains of Synechococcus PCC 7942 were genetically engineered so that copy I of the gene psbA was mutated at specific sites. These mutations resulted in replacements of Ser 264 by Gly or Ala and of Phe 255 by Tyr or Leu in the D 1 protein. The mutants were resistant to herbicides inhibiting electron transfer in photosystem II. All mutants exhibited alterations in the stability of Q B' as demonstrated by a temperature downshift, to various extents, of the in vivo thermoluminescence emission. Measurements of the light-dependent turnover of D 1 showed a marked decrease in the 11 / 2 of this protein in the mutants as compared to wild-type, under low to medium light intensities. A correlation was found between the degree of pertur­ bation in the Q B" stability and the rate of acceleration in the turnover of D 1. These data pro­ vide a direct evidence for the overlapping binding sites for the plastoquinone B and herbicides in the D 1 protein. In addition these data indicate a close link between Q B" destabilization in reaction center II and the mechanism controlling the light-dependent turnover of D 1. Based on these results and previous work we suggest that destabilization of the semireduced quinone, facilitates a light-induced damage in D 1 which triggers its degradation. 
  Reference    Z. Naturforsch. 45c, 402—408 (1990); received November 21 1989 
  Published    1990 
  Keywords    Herbicide Resistance, Thermoluminescence, D 1 Turnover, Synechococcus PCC 7942 
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 TEI-XML for    default:Reihe_C/45/ZNC-1990-45c-0402.pdf 
 Identifier    ZNC-1990-45c-0402 
 Volume    45 
2Author    DirkH. Engels, Anke Engels, ElfriedeK. PistoriusRequires cookie*
 Title    Isolation and Partial Characterization of an l -Amino Acid Oxidase and of Photosystem II Complexes from the Cyanobacterium Synechococcus PCC 7942  
 Abstract    An L-amino acid oxidase with high specifity for basic L-amino acids was isolated from the cyanobacterium Synechococcus PCC 7942, and the enzyme was partially characterized. This enzyme was compared to the previously described L-amino acid oxidase from Synechococcus 
  Reference    Z. Naturforsch. 47c, 859 (1992); received October 4 1992 
  Published    1992 
  Keywords    Cyanobacteria, Synechococcus PCC 7942, Photosystem II, L-Amino Acid Oxidase, Water Oxi­ dizing Enzyme 
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 TEI-XML for    default:Reihe_C/47/ZNC-1992-47c-0859.pdf 
 Identifier    ZNC-1992-47c-0859 
 Volume    47