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  • 1
    Electronic Resource
    Electronic Resource
    Biological Nitrogen Fixation (1978)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Plant Physiology 29 (1978), S. 263-276 
    Details
    ISSN: 0066-4294
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1146/annurev.pp.29.060178.001403
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  • 2
    Electronic Resource
    Electronic Resource
    Proposed nomenclature for the genes involved in molybdenum metabolism in Escherichia coli and Saimonella typhimurium (1992)
    Oxford, UK : Blackwell Publishing Ltd
    Molecular microbiology 6 (1992), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.1992.tb02215.x
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  • 3
    Electronic Resource
    Electronic Resource
    Direct isolation of functional genes encoding cellulases from the microbial consortia in a thermophilic, anaerobic digester maintained on lignocellulose (1995)
    Springer
    Applied microbiology and biotechnology 43 (1995), S. 667-674 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Gene libraries (“zoolibraries”) were constructed in Escherichia coli using DNA isolated from the mixed liquor of thermophilic, anaerobic digesters, which were in continuous operation with lignocellulosic feedstocks for over 10 years. Clones expressing cellulase and xylosidase were readily recovered from these libraries. Four clones that hydrolyzed carboxymethylcellulose and methylumbelliferyl-β-d-cellobiopyranoside were characterized. All four cellulases exhibited temperature optima (60–65° C) and pH optima (pH 6–7) in accordance with conditions of the enrichment. The DNA sequence of the insert in one clone (plasmid pFGH1) was determined. This plasmid encoded an endoglucanase (celA) and part of a putative β-glucosidase (celB), both of which were distinctly different from all previously reported homologues. CelA protein shared limited homology with members of the A3 subfamily of cellulases, being similar to endoglucanase C from Clostridium thermocellum (40% identity). The N-terminal part of CelB protein was most similar to β-glucosidase from Pseudomonas fluorescens subsp. cellulosa (28% homology). The use of zoolibraries constructed from natural or laboratory enrichment cultures offers the potential to discover many new enzymes for biotechnological applications.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00164771
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  • 4
    Electronic Resource
    Electronic Resource
    Direct isolation of functional genes encoding cellulases from the microbial consortia in a thermophilic, anaerobic digester maintained on lignocellulose (1995)
    Springer
    Applied microbiology and biotechnology 43 (1995), S. 667-674 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract  Gene libraries (“zoolibraries”) were constructed in Escherichia coli using DNA isolated from the mixed liquor of thermophilic, anaerobic digesters, which were in continuous operation with lignocellulosic feedstocks for over 10 years. Clones expressing cellulase and xylosidase were readily recovered from these libraries. Four clones that hydrolyzed carboxymethylcellulose and methylumbelliferyl-β-D-cellobiopyranoside were characterized. All four cellulases exhibited temperature optima (60–65 °C) and pH optima (pH 6–7) in accordance with conditions of the enrichment. The DNA sequence of the insert in one clone (plasmid pFGH1) was determined. This plasmid encoded an endoglucanase (celA) and part of a putative β-glucosidase (celB), both of which were distinctly different from all previously reported homologues. CelA protein shared limited homology with members of the A3 subfamily of cellulases, being similar to endoglucanase C from Clostridium thermocellum (40% identity). The N-terminal part of CelB protein was most similar to β-glucosidase from Pseudomonas fluorescens subsp. cellulosa (28% homology). The use of zoolibraries constructed from natural or laboratory enrichment cultures offers the potential to discover many new enzymes for biotechnological applications.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00164771
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  • 5
    Electronic Resource
    Electronic Resource
    Temperature control of nitrogen fixation in Klebsiella pneumoniae (1979)
    Springer
    Archives of microbiology 123 (1979), S. 259-265 
    Details
    ISSN: 1432-072X
    Keywords: Nitrogen fixation ; Nitrogenase ; Gene expression ; Protein synthesis ; Regulation ; Klebsiella pneumoniae ; Microbial ecology
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract At growth temperatures above 37°C, Klebsiella pneumoniae does not grow in a medium containing N2 or NO 3 - as nitrogen sources. However, both the growth in the presence of other nitrogen sources as well as the in vitro nitrogenase activity are not affected at this temperature. The inability to fix N2 at high temperature is due to the failure of the cells to synthesize nitrogenase and other nitrogen fixation (nif) gene encoded proteins. When cells grown under nitrogen fixing conditions at 30°C were shifted to 39°C, there was a rapid decrease of the rate of de novo biosynthesis of nitrogenase (component 1), nitrogenase reductase (component 2), and the nifJ gene product. There was no degradation of nitrogenase at the elevated temperature since preformed enzyme remained stable over a period of at least 3 h at 39°C. Thus, temperature seems to represent a third control system, besides NH 4 + and O2, governing the expression of nif genes of K. pneumoniae.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00406659
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  • 6
    Electronic Resource
    Electronic Resource
    Photoproduction of ammonium ion from N2 inRhodospirillum rubrum (1976)
    Springer
    Archives of microbiology 110 (1976), S. 207-213 
    Details
    ISSN: 1432-072X
    Keywords: Nitrogen fixation ; NH 4 + excretion ; Photosynthesis ; Rhodospirillum rubrum ; Photosynthetic bacteria ; Enzymes of ammonia assimilation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract NH 4 + excretion was undetectable in N2-fixing cultures ofRhodospirillum rubrum (S-1) and nitrogenase activity in these cultures was repressed by the addition of 10 mM NH 4 + to the medium. The glutamate analog,l-methionine-dl-sulfoximine (MSX), derepressed N2 fixation even in the presence of 10 mM extracellular NH 4 + . When 10 mg MSX/ml was added to cultures just prior to nitrogenase induction they developed nitrogenase activity (20% of the control activities) and excreted most of their fixed N2 as NH 4 + . Nitrogenase activities and NH 4 + production from fixed N2 were increased considerably when a combined nitrogen source, NH 4 + (〉40 μmoles NH 4 + /mg cell protein in 6 days) orl-glutamate (〉60 μmoles NH 4 + /mg cell protein in 6 days) was added to the cultures together with MSX. Biochemical analysis revealed thatR. rubrum produced glutamine synthetase and glutamate synthase (NADP-dependent) but no detectable NADP-dependent glutamate dehydrogenase. The specific activity of glutamine synthetase was observed to be maximal when nitrogenase activity was also maximal. Nitrogenase and glutamine synthetase activities were repressed by NH 4 + as well as by glutamate. The results demonstrate that utilization of solar energy to photoproduce large quantities of NH 4 + from N2 is possible with photosynthetic bacteria by interfering with their regulatory control of N2 fixation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00690229
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  • 7
    Electronic Resource
    Electronic Resource
    Molybdate transport and regulation in bacteria (1997)
    Springer
    Archives of microbiology 168 (1997), S. 345-354 
    Details
    ISSN: 1432-072X
    Keywords: Key words Molybdate transport ; modABC Genes ; modE Gene ; Molybdate-specific repressor ; ABC ; transport system ; Molybdate transport/genetics/ ; regulation ; Escherichia coli ; Azotobacter vinelandii ; Rhodobacter capsulatus ; Clostridium pasteurianum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Molybdate is transported in bacteria by a high-affinity transport system composed of a periplasmic binding protein, an integral membrane protein, and an energizer protein. These three proteins are coded by modA, modB, and modC genes, respectively. The ModA, ModB, and ModC proteins from various organisms (Escherichia coli, Haemophilus influenzae, Azotobacter vinelandii, and Rhodobacter capsulatus) are very similar. The lowest K m value reported for molybdate in the molybdate transport process is approximately 50 nM. In a mod mutant, molybdate is transported by the sulfate transport system or by a nonspecific anion transporter. Molybdate transport is tightly coupled to utilization in E. coli and Klebsiella pneumoniae, while other dinitrogen-fixing organisms appear to have a molybdenum storage protein. In all organisms studied so far, molybdate transport genes are regulated by a repressor protein, ModE. The ModE-molybdate complex binds to the sequences TAYAT (Y = T or C) in the operator/ promoter region in E. coli and prevents transcription of the modABCD operon. The ModE-molybdate complex binds to DNA as a homodimer in E. coli and possibly in other organisms as well. In R. capsulatus, however, two ModE homologues (MopAB proteins) are required for repression.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002030050508
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  • 8
    Electronic Resource
    Electronic Resource
    Mechanism of catalase induction in Rhodopseudomonas spheroides: Role of porphyrin excretion (1969)
    Springer
    Archives of microbiology 69 (1969), S. 197-205 
    Details
    ISSN: 1432-072X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Catalase induction in Rhodopseudomonas spheroides and three locally isolated strains of Rhodopseudomonas (TL-1, TL-4 and Rps. D) was studied. A correlation between the rate of excretion of porphyrin and the inducibility of the culture was observed. 8-hydroxyquinoline at 4x10-5 M had no effect on Bchl synthesis but it inhibited porphyrin excretion and catalase induction in Rhodopseudomonas spheroides. 8-OH Q at this concentration partially inhibited Bchl synthesis and catalase induction in strain TL-1. The data indicate that the amount of catalase produced is dependent on the pool size of porphyrins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00408972
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  • 9
    Electronic Resource
    Electronic Resource
    Mechanism of catalase induction in Rhodopseudomonas spheroides: The effects of acridine, acriflavin, and diphenylamine (1969)
    Springer
    Archives of microbiology 69 (1969), S. 206-215 
    Details
    ISSN: 1432-072X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The effect of inhibitors of carotenoid synthesis, diphenylamine, acridine, and acriflavin on catalase induction was studied in Rhodopseudomonas spheroides. The induction of catalase by 40 μM H2O2, was inhibited 5x10-4 M acridine, 5 μM acriflavin and 3x10-4 diphenylamine. Acridine, acriflavin and diphenylamine at 1.0x10-4 M, 1.5 μM and 5x10-5 M respectively, stimulated the induction. The stimulatory effect was shown to be at the transcriptional level rather than at the translational level. The concentration of acridine which stimulated the induction of the enzyme inhibited general protein synthesis in the cell, under similar conditions. Acriflavin also did not stimulate the induction of β-galactosidase in Escherichia coli B. It is suggested that these acridine dyes interact with the internal inducer-DNA complex which leads to a higher rate of production of catalase mRNA.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00408973
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  • 10
    Electronic Resource
    Electronic Resource
    Nif-hybrids of enterobacter: Selection for nif gene integration with chlorate (1983)
    Springer
    Molecular genetics and genomics 191 (1983), S. 221-224 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The nif gene group from Klebsiella can be transferred into Enterobacter cloacae by conjugation using Escherichia coli donor cells carrying the composite self-transmissible nif-plasmid pRD1. A small fraction of the hybrids obtained is stable upon prolonged passaging without selection. Their stability is due to integration of pRD1 into the chromosome. Such integration hybrids were chlorate resistant, and nitrate reductase negative, which indicated that integration preferentially occurred within one of the genes for the production or functioning of this enzyme. Chlorate resistance could, therefore, be used to select for additional nitrate reductase-negative sublines with pRD1 in their chromosome. Such sublines have been analyzed further for the presence of nif genes, other pRD1 markers, and for stability. In all except one the complete plasmid seems to have been integrated. Some tend to revert to nitrate utilisation (chlorate sensitivity).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00334817
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