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21Author    Gudrun Wälzlein, AchimE. Gau, ElfriedeK. PistoriusRequires cookie*
 Title    Further Investigations about the Flavin in the L-Amino Acid Oxidase and a Possible Flavin in Photosystem II Complexes from the Cyanobacterium Anacystis nidulans  
 Abstract    The absorption spectrum of the previously purified L-amino acid oxidase from the cyanobac-terium Anacystis nidulans has shown considerable variation with each preparation and the spec-trum in several preparations was quite different from the absorption spectrum of other simple flavoproteins (E. K. Pistorius and A. E. Gau, Biochim. Biophys. Acta 849, 203, 1986). Here we show that the spectral complexity and variability of the L-amino acid oxidase can be largely explained by the presence of a modified flavin derivative of yet unknown structure besides oxidized FAD and FAD semiquinone. After removal from the enzyme this modified chromophore has absorption maxima at 260, 396 and in the 600 nm region. This derivative of FAD seems to be formed in variable amounts during the purification of the enzyme. On the other hand, extraction of Anacystis photosystem II complexes which contain the flavoprotein, almost exclusively yields modified flavin derivatives and practically no authentic oxidized FAD. The spectrum of the chromophores which have been extracted from photosystem II complexes at different purification stages, is either similar (although not identical) to the spectrum of the chromophore extracted from the isolated L-amino acid oxidase or similar to the spectrum of reduced flavin. All extracted chromophores show a fluorescence emission in the 420 to 560 nm region when excited with light of 390 nm. These results indicate that the flavin present in the L-amino acid oxidase protein as well as in photosystem II complexes from A. nidulans rapidly undergoes modification reactions of yet unknown nature to yield several closely related FAD derivatives. This might possibly be the reason why so far no flavin has been detected in photosys-tem II. The presence of such modified flavin derivatives in photosystem II complexes of A. nidulans as shown here is an additional support of our hypothesis that an unusual flavin is functional on the donor side of photosystem II. 
  Reference    Z. Naturforsch. 43c, 545—553 (1988); received January 25 1988 
  Published    1988 
  Keywords    L-Amino Acid Oxidase, Flavoprotein, Photosystem II, Cyanobacteria, Anacystis nidulans 
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 TEI-XML for    default:Reihe_C/43/ZNC-1988-43c-0545.pdf 
 Identifier    ZNC-1988-43c-0545 
 Volume    43 
22Author    AchimE. Gau, Gudrun Wälzlein, Susanne Gärtner, Matthias Kuhlmann, Susanne Specht, ElfriedeK. PistoriusRequires cookie*
 Title    Immunological Identification of Polypeptides in Photosystem II Complexes from the Cyanobacterium Anacystis nidulans  
 Abstract    Photosystem II complexes from the cyanobacterium Anacystis nidulans have been investigated by Western blots with antisera raised against four photosystem II peptides from plants and with an antiserum raised against the soluble L-amino acid oxidase protein from/1. nidulans to achieve an iden­ tification of the polypeptides — especially of the L-amino acid oxidase related protein — in isolated photosystem II complexes. Anacystis photosystem II complexes which were solubilized with lauryldimethylamine N-oxide and purified by sucrose cushion and sucrose gradient centrifugation, contained as major Coomassie brilliant blue stained polypeptides a 71 kDa band of unknown identity, a 62 kDa band, which partly contained D-l, a 55 and 49 kDa band which were immuno-reactive with an antiserum to the 47 kDa peptide of tobacco PS II complexes, and three distinct bands in the 30 kDa region. These latter bands could be identified as the extrinsic Mn stabilizing peptide (27—30 kDa), D-l (30—33 kDa) and a 36 kDa peptide (35 — 38 kDa) which crossreacted with the antiserum raised against the soluble L-amino acid oxidase protein of 50 kDa. These results suggest that the 36 kDa peptide present in purified photosystem II complexes from A. nidulans might be a processed form of the soluble 50 kDa L-amino acid oxidase protein. 
  Reference    Z. Naturforsch. 44c, 971—975 (1989); received June 22 1989 
  Published    1989 
  Keywords    Photosystem II, L-Amino Acid Oxidase, Antibody, Cyanobacteria, Anacystis nidulans 
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 TEI-XML for    default:Reihe_C/44/ZNC-1989-44c-0971.pdf 
 Identifier    ZNC-1989-44c-0971 
 Volume    44 
23Author    G. Ajlani, I. Meyer, C. Astier, C. VernotteRequires cookie*
 Title    Inhibition of Photosystem II by Ioxynil in Wild Type and Resistant Mutant of Synechocystis 6714  
 Abstract    A Synechocystis 6714 mutant resistant to the phenol-type herbicide ioxynil was isolated and characterized. Ioxynil was shown to inhibit both the donor and the acceptor sides of photosystem II, but at different concentrations. The mutation found in the psbA gene (encoding the D, protein) at codon 266 (asparagine to threonine) [G. Ajlani, I. Meyer, C. Vernotte, and C. Astier, FEBS Lett. 246, 207—210 (1989)] gives a ten-fold resistance of the acceptor side to ioxynil without any modification of the sensitivity of the donor side. Electron transfer between the primary and the secondary acceptor of photosystem II was identical in the mutant and the wild type. The mutant remains sensitive to atrazine and is even more sensitive to D C M U than the wild type. 
  Reference    Z. Naturforsch. 44c, 979 (1989); received June 16 1989 
  Published    1989 
  Keywords    Phenolic Herbicide, Ioxynil, Photosystem II, Cyanobacteria, D i Protein 
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 TEI-XML for    default:Reihe_C/44/ZNC-1989-44c-0979.pdf 
 Identifier    ZNC-1989-44c-0979 
 Volume    44 
24Author    Hartmut Spiller, Anneliese Ernst, Wolfgang Kerfin, Peter BögerRequires cookie*
 Title    Increase and Stabilization of Photoproduction of Hydrogen in Nostoc muscorum by Photosynthetic Electron Transport Inhibitors  
 Abstract    Nittrogen-fixing cells of N o s to c m u s co ru m grown under nitrogen or in the presence of nitrate exhibit substantial light-induced hydrogen production for over 15 hours in the presence of electron transport inhibitors. Rates attain levels of 12 //mol H 2 evolved/ml packed cell volume and hour. The ATP-dependent nitrogenase, not a hydrogenase, is responsible for hydrogen production. This is indicated by poor sensitivity to CO and inhibition of the reaction by uncouplers, acetylene, and N 2 . A n active uptake hydrogenase minimizes light-induced H 2 production. Although nitrogenase activity is somewhat decreased by several photosynthetic electron transport inhibitors, hydrogen production is markedly increased. This is due to lowering the partial pressure of oxygen in the cell, preventing oxidative hydrogen consumption. 
  Reference    Z. Naturforsch. 33c, 541 (1978); received M ay 24 1978 
  Published    1978 
  Keywords    Cyanobacteria, W ater Photolysis, Nitrogenase, Uptake Hydrogenase, Photoproduction of Hydrogen, Photosynthetic Electron Transport Inhibitors 
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 TEI-XML for    default:Reihe_C/33/ZNC-1978-33c-0541.pdf 
 Identifier    ZNC-1978-33c-0541 
 Volume    33 
25Author    Anneliese Ernst, Wolfgang Kerfin, Hartmut Spiller, Peter BögerRequires cookie*
 Title    External Factors Influencing Light-Induced Hydrogen Evolution by the Blue-Green Alga, Nostoc muscorum  
 Abstract    This study was conducted to determine some physiological conditions which influence light-in­ duced hydrogen evolution by intact cells of the blue-green alga Nostoc muscorum. This activity was found to be dependent on the age of the culture, cultivation temperature, ageing of the cells, and on gassing the cultures with nitrogen or air. Nitrogenase is particularly ac­ tive after cultivation at 22 °C but not at 32 °C although growth is about the same. The molar ratio of acetylene reduction to hydrogen evolution -both gas exchanges obviously catalyzed by nitrogen­ ase -is also dependent on age and temperature of the culture. A hydrogen-consuming ("up­ take") hydrogenase activity is present and affected by prolonged microaerobic, but not by aerobic growth conditions, and stimulated by light. External factors during growth apparently influence differently the activities of nitrogenase and uptake hydrogenase. Consequently -besides the electron donor supply -net light-induced hydro­ gen evolution by intact cells is dependent on these two variable activities. 
  Reference    Z. Naturforsch. 34c, 820 (1979); received May 8/June 11 1979 
  Published    1979 
  Keywords    Photoproduction of Hydrogen, Cyanobacteria, Heterocysts, Water Photolysis, Nitrogenase, Uptake Hydrogenase 
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 TEI-XML for    default:Reihe_C/34/ZNC-1979-34c-0820.pdf 
 Identifier    ZNC-1979-34c-0820 
 Volume    34 
26Author    Siegfried Scherer, Peter BögerRequires cookie*
 Title      
 Abstract    As reported in the literature, ferricyanide reduction o f blue-green algal cells in the dark is linked to respiratory electron transport. This study has not verified this hyp o­ thesis. There was no concurrent activity o f ferricyanide reduction by intact cells with respiratory oxygen uptake. It was found light-independent, showing little K CN-in-hibition, but was strongly CCCP-sensitive. CCCP inh ib i­ tion was reversed by KCN. -Both, respiration and ferri­ cyanide reduction were stimulated by fructose which was actively accumulated by the cells (the apparent K m was 20 |iM). Ferricyanide reduction was more sensitive towards dark starvation than respiration. Based on these data it is suggested that ferricyanide reduction and cyanide-sensitive respiration are parts o f different electron-transport pro­ cesses, competing for reduction equivalents originating from the same (endogenous) carbon pool. 
  Reference    Z. Naturforsch. 40c, 138—141 (1985); received December 12 1984 
  Published    1985 
  Keywords    Cyanobacteria, Anabaena, Respiratory Electron Transport, Cytoplasmic Membrane, Ferricyanide R eduction, K m, ' Fructose Uptake 
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 TEI-XML for    default:Reihe_C/40/ZNC-1985-40c-0138_n.pdf 
 Identifier    ZNC-1985-40c-0138_n 
 Volume    40 
27Author    Joseph Hirschberg, NirO. Had, Iris Pecker, Ana RahatRequires cookie*
 Title    Isolation and Characterization of Herbicide Resistant Mutants in the Cyanobacterium Synechococcus R2  
 Abstract    Departm ent o f G en etics, The H ebrew University o f Jerusalem. Jerusalem. A variety of mutants which are resistant to triazine — and urea — classes of herbicides have been isolated in the cyanobacterium Synechococcus R 2. A ll the mutants that have been analyzed, show som e cross-resistance to different herbicides suggesting that these herbicides share a com m on binding site in photosystem II. Three psbA genes have been identified in Synechococcus R 2. The /« M -c o p y I gene was cloned from three mutants and used in D N A -m ed iated genetic transformation. It was found that in all three mutants this gene could transfer the mutation for herbicide resistance indicating that this gene codes for the herbicide resistant protein. 
  Reference    Z. Naturforsch. 42c, 758—7 (1987); received January 7 1987 
  Published    1987 
  Keywords    H erbicide Resistance, psb A G en e, Photosystem II, Cyanobacteria, Mutants 
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 TEI-XML for    default:Reihe_C/42/ZNC-1987-42c-0758.pdf 
 Identifier    ZNC-1987-42c-0758 
 Volume    42 
28Author    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 
29Author    Gudrun Wälzlein, ElfriedeK. PistoriusRequires cookie*
 Title    Inactivation of Photosynthetic 0 2 Evolution in the Cyanobacterium Anacystis nidulans PCC 6301: Influence of Nitrogen Metabolites and Divalent Cation Concentration  
 Abstract    A n investigation about the in vivo inactivation o f photosynthetic water oxidation has been carried out in the cyanobacterium Anacystis nidulans (Synechococcus PC C 6301). Photosystem II and photosystem I activity as well as the relative am ount of the D 1 and manganese stabiliz­ ing peptide o f photosystem II were determined after growing the cells in nutrient media with variations in the nitrogen source and the concentration of the major divalent cations (M g 2+ and C a :+). The results show a rapid inactivation of water oxidation in A. nidulans in response to nitrogen deficiency and in response to reduced M g:+ and C a2+ concentrations. The inactiva­ tion o f water oxidation observed under divalent cation deficiency could be greatly accelerated when L-amino acids instead o f am m onia or nitrate were used as nitrogen source. Under these conditions inactivation o f water oxidation correlated with a rapid loss o f D 1 and with a slower loss o f the manganese stabilizing peptide from photosystem II. A possible regulation o f the photosystem II activity in A. nidulans by nitrogen metabolites is suggested. 
  Reference    Z. Naturforsch. 46c, 1024—1032 (1991); received June 26/August 19 1991 
  Published    1991 
  Keywords    Cyanobacteria, Anacystis nidulans PCC6301, Synechococcus PCC6301, Photosystem II, Photosystem I, Nitrogen Metabolism 
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 TEI-XML for    default:Reihe_C/46/ZNC-1991-46c-1024.pdf 
 Identifier    ZNC-1991-46c-1024 
 Volume    46 
30Author    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 
31Author    Klaus-Peter Michel, ElfriedeK. Pistorius, E. Gau, G. Wälzlein, S. Gärtner, M. Kuhlmann, E. K. PistoriusRequires cookie*
 Title    Isolation of a Photosystem II Associated 36 kDa Polypeptide and an Iron-Stress 34 kDa Polypeptide from Thylakoid Membranes of the Cyanobacterium Synechococcus PCC 6301 Grown under Mild Iron Deficiency  
 Abstract    A 36 kDa polypeptide which previously was shown to be present in purified photosystem II complexes from Synechococcus PCC 6301 and which crossreacts with the antiserum raised against the soluble L-amino acid oxidase o f 50 kD a from Synechococcus PCC 6301 (A. was isolated from thylakoid membranes o f the same cyanobacterium grown under mild iron deficiency. This peptide is present in about equal am ounts in thylakoid membranes o f Syne­ chococcus PCC 6301 grown under regular or iron deficient conditions. The antiserum raised against this thylakoid membrane bound 36 kD a peptide crossreacts with the soluble L-amino acid oxidase o f 50 kDa. These results further support our conclusion that the thylakoid mem­ brane bound 36 kD a polypeptide is a modified form o f the soluble 50 kD a L-amino acid oxi­ dase. In addition, a 34 kD a polypeptide was isolated from iron stressed thylakoid membranes, and an antiserum was also raised against this protein. Im m unoblot experiments with this an­ tiserum show that the 34 kD a peptide is present in elevated amounts in thylakoid membranes from Synechococcus cells grown under iron deficiency and that it is alm ost absent in thylakoid membranes from cells grown under regular conditions. 
  Reference    Z. Naturforsch. 47c, 867—8 (1992); received August 4/O ctober 8 1992 
  Published    1992 
  Keywords    Cyanobacteria, Synechococcus PCC 6301, Photosystem II, L-Amino Acid Oxidase, Iron Stress 
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 TEI-XML for    default:Reihe_C/47/ZNC-1992-47c-0867.pdf 
 Identifier    ZNC-1992-47c-0867 
 Volume    47 
32Author    Ulrich SchreiberRequires cookie*
 Title    New Emitter-Detector-Cuvette Assembly for Measuring Modulated Chlorophyll Fluorescence of Highly Diluted Suspensions in Conjunction with the Standard PAM Fluorometer  
 Abstract    A new emitter-detector-cuvette assembly for the standard PAM fluorometer is described which leads to substantial improvement of signal/noise ratio and increased flexibility with respect to the choice of excitation and emission wavelengths. These features are particularly useful for work with very dilute suspensions of unicellular algae and isolated chloroplasts. Instead of fiber optics perspex rods are applied for guiding excitation light to a mirrored 10x10x45 mm cuvette and from there at 90° angle to the photodetector, similarly as recently reported for a PAM fluorometer based on Xe-flash measuring light (Schreiber et al. (1993), Photosynth. Res. 36, 65-72). While the detection limit of the new system does not reach that of the Xe-PAM fluorometer, it is approximately two orders of magnitude higher than that of the standard system. Rapid induction kinetics can be measured at low chlorophyll concen­ trations down to 0.1 (.ig-ml '. Satisfactory quenching analysis for detection of active chloro­ phyll concentration is still possible at 5 |ig chlorophyllT '. The various optical factors con­ tributing to the improved sensitivity are analyzed. An accessory device is described by which the frequency of the measuring light pulses generated by the PAM fluorometer is lowered in order to reduce the actinic effect of the measuring light. The performance of the new system using different excitation and emission wavelengths is demonstrated in measurements with green algae, cyanobacteria and leaves. Applying a newly available blue light-emitting diode with 450 nm peak emission, short wavelength fluorescence enriched in PS II emission can be measured, which is characterized by high values of variable fluorescence relative to maximal fluorescence. Using measuring light covering five different wavelength ranges the fluorescence contributions from cyanobacteria and green algae can be distinguished on the basis of distinct differences in their excitation spectra. This approach should become useful for an estimation of content and activity of different types of phytoplankton in natural surface waters. 
  Reference    Z. Naturforsch. 49c, 646—656 (1994); received May 18/July 7 1994 
  Published    1994 
  Keywords    Chlorophyll Fluorescence, Photosynthesis, PAM Fluorometer, Quenching Analysis, Unicellular Algae, Cyanobacteria, Phytoplankton 
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 TEI-XML for    default:Reihe_C/49/ZNC-1994-49c-0646.pdf 
 Identifier    ZNC-1994-49c-0646 
 Volume    49 
33Author    K. Burda, G. H. SchmidRequires cookie*
 Title    On the Determination of the 5-State Distribution in the Kok Model  
 Abstract    We use the Markow chain theory to analyze the oscillation pattern of oxygen evolution during water oxidation in photosystem II under short saturating light flashes. We propose a method based on the standard least square deviation (test x 2) to determine the number of 5-states in the Kok model. As pointed out by Burda et al. (1995) this information is amongst others important for the interpretation of the role of calcium for oxygen evolution. A specific mathematical representation for a situation when the S4 state is longer living than generally assumed is introduced which requires an explicit extension of the Kok model to five states. The higher stability is modelled by introducing additional decay channels, e.g. a nonvanishing probability for the transition of S3 to the 5() state and a further transition probability for the transition from S3 to 5 4. Our analysis is extended to the case of damped oscillations of oxygen evolution caused, for example, by the lack of electron acceptor or the short life time of photosystem II particles. 
  Reference    Z. Naturforsch. 51c, 329—341 (1996); received O ctober 23/D ecem ber 5 1995 
  Published    1996 
  Keywords    0 2-Evolution, o-and ^-Analysis, Transition Probabilities, Cyanobacteria, Tobacco, Chlorella 
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 TEI-XML for    default:Reihe_C/51/ZNC-1996-51c-0329.pdf 
 Identifier    ZNC-1996-51c-0329 
 Volume    51 
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