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1Author    Wolfgang Lockau, Susanne PfefferRequires cookie*
 Title    A Cyanobacterial ATPase Distinct from the Coupling Factor of Photophosphorylation  
 Abstract    A particle-bound, M g2+-dependent A TPase activity is investigated in cell-free extracts o f the cyanobacterium Anabaena variabilis. The enzym e can be clearly distinguished from the 
  Reference    Z. Naturforsch. 37c, 658 (1982); received March 231982 
  Published    1982 
  Keywords    Cyanobacterium, Anabaena variabilis, ATPase, Coupling Factor, Cytochrom e Oxidase 
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 TEI-XML for    default:Reihe_C/37/ZNC-1982-37c-0658.pdf 
 Identifier    ZNC-1982-37c-0658 
 Volume    37 
2Author    Ulrike Strohmeier, ChristianG. Erdes3, Wolfgang LockaubRequires cookie*
 Title    Proteolysis in Heterocyst-Forming Cyanobacteria: Characterization of a Further Enzyme with Trypsin-Like Specificity, and of a Prolyl Endopeptidase from Anabaena variabilis  
 Abstract    of the cyanobacterium Anabaena variabilis ATCC 29413 and an en­ gineered mutant that lacks an intracellular protease cleaving after Lys and Arg (Maldener, Lockau, Cai, and Wolk, Mol. Gen. Genet. 225, 113-120 (1991)) were separated by ion ex­ change chromatography, and protease profiles determined using azocasein, Na-benzoyl-D,L-arginine-4-nitroanilide and N-carbobenzoxy-glycyl-L-proline-4-nitroanilide as substrates. A second enzyme cleaving at the carboxyl side of lysine and arginine, and a prolyl endopepti­ dase were detected, enriched and characterized. Both proteolytic enzymes appear to be located in the periplasm. 
  Reference    Z. Naturforsch. 49c, 70—78 (1994); received September 29/December 81993 
  Published    1994 
  Keywords    Anabaena variabilis, Cyanobacterium, Heterocysts, Proteolytic Enzymes, Prolyl Endopeptidase Soluble extracts 
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 TEI-XML for    default:Reihe_C/49/ZNC-1994-49c-0070.pdf 
 Identifier    ZNC-1994-49c-0070 
 Volume    49 
3Author    ShigetohM. Iyachi11, JoachimB. Ürger, K. Iriakos, K. Otzabasisb, JensT. Hielm Annc, H. O. Rst SengerRequires cookie*
 Title    Photosynthetic Characteristics of Three Strains of Cyanobacteria Grown under Low-or High-C02 Conditions  
 Abstract    Quantum requirements of photosynthetic oxygen evolution at 679 nm, fluorescence em is­ sion spectra at liquid nitrogen temperature (77 K) and fluorescence induction kinetics in the presence of DCM U, were measured in the cyanobacteria Anabaena variabilis M3, Anabaena variabilis ATCC 29413 and A nacystis nidulans R2, each grown under low-or high-C02 condi­ tions. L o w -C 0 2 grown cells o f the cyanobacteria showed a higher quantum requirement of photosynthetic oxygen evolution and a higher ratio o f F7U)_740 to F680_700 fluorescence and a lower variable fluorescence in the presence of D CM U than high-C02 grown cells. These findings indicate a change in excitation energy distribution in favour of photosystem I. The result might be an enhancement in ATP formation caused by cyclic electron flow which in turn provokes dissolved inorganic carbon (D IC) accumulation in these low-C02 grown cells. 
  Reference    Z. Naturforsch. 51c, 40—4 (1996); received August 4/October 6 1995 
  Published    1996 
  Keywords    Quantum Requirement, Fluorescence, Dissolved Inorganic Carbon, Anabaena variabilis, Anacystis nidulans 
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 TEI-XML for    default:Reihe_C/51/ZNC-1996-51c-0040.pdf 
 Identifier    ZNC-1996-51c-0040 
 Volume    51 
4Author    T. Kentemich, G. Haverkam, H. BotheRequires cookie*
 Title    The Expression of a Third Nitrogenase in the Cyanobacterium Anabaena variabilis  
 Abstract    Physiological experiments indicate that Anabaena variabilis can express either a V-or a Fe-nitrogenase in addition to the conventional, M o-containing enzyme complex. The occur­ rence o f the Fe-nitrogenase in A. variabilis can also be concluded from D N A -D N A hybridiza­ tion experiments using cloned anfW or nifW probes coding for the smaller subunit (= nitroge­ nase reductase) o f the Fe-nitrogenase from Azotobacter vinelandii or for the same subunit o f the M o-nitrogenase from Klebsiella pneumoniae. The cyanobacterium A. variabilis is the first phototroph found to contain all three nitrogenases landii as yet. Vanadium cannot substitute for M o in 
  Reference    Z. Naturforsch. 46c, 217 (1991); received November 2 1990 
  Published    1991 
  Keywords    Alternative N itrogenases, Vanadium-Nitrogenase, Iron-Nitrogenase, Nitrate Reduction, Cyanobacteria, Anabaena variabilis 
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 TEI-XML for    default:Reihe_C/46/ZNC-1991-46c-0217.pdf 
 Identifier    ZNC-1991-46c-0217 
 Volume    46 
5Author    Gottfried Martin, Peter BögerRequires cookie*
 Title    Two Ways of Hydrogen Peroxide Formation in the Oxidative Inactivation of Cyanobacterial Glutamine Synthetase  
 Abstract    Using crude extracts from the cyanobacterium Anabaena variabilis glutamine synthetase (GS) activity was rapidly irreversibly reduced to about 60% during dark incubation ("sponta­ neous GS inactivation"). An additional decrease was observed by the addition of ammonia in the light ("ammonia-m ediated inactivation"). Both effects were prevented by EDTA, MnCl2 or catalase indicative of the involvement of H 20 2. This is a key interm ediate in oxida­ tive enzyme inactivation. In both spontaneous and am monia-mediated GS inactivation H 20 2 is produced in different ways. Spontaneous inactivation is prevented by depletion of reduced pyridine nucleotides which apparently donate electrons to produce H 20 2. Fractionation of the crude extract showed that the light-enhanced GS inactivation by ammonia required the presence of thylakoid membranes. The photosynthesis inhibitor DCM U decreased GS inacti­ vation by ammonia. For the inactivation in the light apparently H 20 2 is produced from super­ oxide during photosynthetic electron transport. 
  Reference    Z. Naturforsch. 52c, 812—816 (1997); received August 12 1997 
  Published    1997 
  Keywords    Glutamine Synthetase, Protein Oxidation Ammonia Effect, Photosynthetic Hydrogen Peroxide Production, Cyanobacterium, Anabaena variabilis 
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 TEI-XML for    default:Reihe_C/52/ZNC-1997-52c-0812.pdf 
 Identifier    ZNC-1997-52c-0812 
 Volume    52