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'Cyanobacteria' in keywords Facet   Publication Year 1990  [X]
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1990[X]
1Author    A.-KJ. Sallal, N. A. NimerRequires cookie*
 Title    The Presence of Malate Dehydrogenase in Thylakoids of Anabaena cylindrical Nostoc muscorum and Chlorogloeopsis fritschii  
 Abstract    The location o f malate dehydrogenase in the cyanobacteria, Anabaena cylindrica, Nostoc muscorum and Chlorogloeopsis fritsch ii was investigated by the fractionation o f cell-free ex­ tracts. The bulk o f the enzyme activity was associated with the thylakoid membrane fraction, which also exhibited complete photosynthetic electron transport reactions. Malate dehydro­ genase activity and photosystem II activities were inhibited by hom ologous antisera raised against isolated thylakoid membranes. 
  Reference    Z. Naturforsch. 45c, 249 (1990); received July 4/O ctober 13 1989 
  Published    1990 
  Keywords    Cyanobacteria, Malate Dehydrogenase, Thylakoids 
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 TEI-XML for    default:Reihe_C/45/ZNC-1990-45c-0249.pdf 
 Identifier    ZNC-1990-45c-0249 
 Volume    45 
2Author    Wim Vermaas, Jeroen Charité, Gaozhong ShenRequires cookie*
 Title    Q a Binding to D2 Contributes to the Functional and Structural Integrity of Photosystem II  
 Abstract    Two D 2 mutants were created with a site-directed mutation near the presumable binding site of Q a. In one of the mutants, in which Trp-253, the aromatic residue potentially involved in facilitating electron transport from pheophytin to Q A and/or in binding of Q A, had been replaced by Leu, PS II was undetectable in thylakoids. This mutant is an obligate photohetero-troph. In another mutant the Gly-215 residue, located next to the His residue that is pro­ posed to bind Q a and Fe2+, was mutated to Trp. This mutation leads to a rapid inactivation of oxygen evolution capacity in the light, and to a virtual elimination of the potential to grow photoautotrophically, but does not greatly affect the number of photosystem II reaction cen­ ters on a chlorophyll basis. We propose that proper binding of Q A to the photosystem II reac­ tion center complex is a prerequisite for stability of the photosystem II complex. Impairment of Q a binding leads to rapid inactivation of photosystem II, which may be followed by a struc­ tural disintegration of the complex. 
  Reference    Z. Naturforsch. 45c, 359—365 (1990); received November 3 1989 
  Published    1990 
  Keywords    Photoinhibition, Plastoquinone, Photosynthesis, Site-Directed Mutagenesis, Cyanobacteria 
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 TEI-XML for    default:Reihe_C/45/ZNC-1990-45c-0359.pdf 
 Identifier    ZNC-1990-45c-0359 
 Volume    45