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  • 27.80.+w  (3)
  • Pseudomonas carboxydovorans  (3)
  • Springer  (6)
  • Blackwell Publishing Ltd
  • Nature Publishing Group
  • Oxford University Press
  • 2020-2024
  • 1990-1994  (6)
  • 1965-1969
  • 1960-1964
Collection
Keywords
Publisher
  • Springer  (6)
  • Blackwell Publishing Ltd
  • Nature Publishing Group
  • Oxford University Press
Years
Year
  • 1
    Electronic Resource
    Electronic Resource
    New results on the superdeformed band in192Hg (1994)
    Springer
    The European physical journal 347 (1994), S. 223-224 
    Details
    ISSN: 1434-601X
    Keywords: 21.10.Re ; 23.20.Lv ; 27.80.+w
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract New results on the192Hg superdeformed band have been obtained with EUROGAM. The experiment has been performed with the160Gd(36S,4n) reaction at 159 MeV. Above 800 keV the γ-ray energies differ from the previously published ones. Thus the rise of the dynamical moment of inertia $$\mathfrak{F}^{(2)} $$ above ħω=0.4 MeV is no longer observed. This is in better agreement with recent cranked Hartree-Fock-Bogoliubov calculations.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01292380
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  • 2
    Electronic Resource
    Electronic Resource
    First observation of a superdeformed nucleus produced in an α xn reaction channel (1994)
    Springer
    The European physical journal 349 (1994), S. 5-6 
    Details
    ISSN: 1434-601X
    Keywords: 21.10.Re ; 23.20.Lv ; 27.80.+w
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract Recent data from the EUROGAM array have revealed the population of the yrast superdeformed (SD) band of192Hg in the α4n exit channel of the16O+184W reaction at 113 MeV beam energy. The nucleus assignment was made on the basis of the SD band transition energies, and the observation of characteristic X-rays and lowlying yrast γ-transition of192Hg in coincidence with the SD band γ-rays. Both the feeding and decay-out patterns of the observed SD band have been found similar to the ones previously measured in the (36S,4n) reaction.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01296325
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  • 3
    Electronic Resource
    Electronic Resource
    Nitrate respiration, denitrification, and utilization of nitrogen sources by aerobic carbon monoxide-oxidizing bacteria (1990)
    Springer
    Archives of microbiology 154 (1990), S. 168-174 
    Details
    ISSN: 1432-072X
    Keywords: CO ; Nitrite ; Nitrous oxide ; Nitrogen assimilation ; Carboxydotrophic bacteria ; Pseudomonas carboxydoflava ; Pseudomonas carboxydohydrogena ; Pseudomonas carboxydovorans
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We describe the ability of carboxydotrophic bacteria for nitrate respiration or denitrification. Four out of fourteen strains examined could denitrify heterotrophically forming N2 (Pseudomonas carboxydoflava) or N2O (Pseudomonas carboxydohydrogena, Pseudomonas compransoris, and Pseudomonas gazotropha). Three carried out a heterotrophic nitrate respiration (Arthrobacter 11/x, Azomonas B1, and Azomonas C2). P. carboxydohydrogena could use H2 as electron donor for nitrate respiration under chemolithoautotrophic growth conditions. CO did not support denitrification or nitrate respiration of carboxydotrophic bacteria, although the free energy changes of the reactions would be sufficiently negative to allow growth. CO at 50 kPa was a weak inhibitor of N2O-reduction in carboxydotrophic and non-carboxydotrophic bacteria and decelerated denitrifying growth. Carboxydotrophic bacteria could utilize a wide range of N-sources. Results obtained with a plasmid-cured mutant of Pseudomonas carboxydovorans OM5 showed, that genes involved in nitrogen assimilation entirely reside on the chromosome. In the presence of an suitable electron donor, most carboxydotrophic bacteria could carry out a reduction of nitrate to nitrite that did not support growth and did not lead to the formation of ammonia.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00423328
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  • 4
    Electronic Resource
    Electronic Resource
    Genes encoding ribulosebisphosphate carboxylase and phosphoribulokinase are duplicated in Pseudomonas carboxydovorans and conserved in carboxydotrophic bacteria (1991)
    Springer
    Archives of microbiology 157 (1991), S. 92-96 
    Details
    ISSN: 1432-072X
    Keywords: Carboxydotrophic bacteria ; Ribulosebis-phosphate carboxylase ; Phosphoribulokinase ; Hybridization ; Plasmids ; Genetics ; CO2 fixation ; Alcaligenes eutrophus ; Pseudomonas carboxydovorans ; Rhodospirillum rubrum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Heterologous gene probes derived from cfxLp and cfxPp genes of Alcaligenes eutrophus H16 revealed the presence of structural genes encoding ribulosebisphosphate carboxylase (Rubisco) and phosphoribulokinase (PRK) on the genome of carboxydotrophic bacteria. The two genes were found to be rather conserved. In Pseudomonas carboxydovorans OM5 cfx genes reside on the plasmid pHCG3 and the chromosome as well, indicating that they are duplicated. Also in all plasmidharboring carboxydotrophic bacteria cfxL and cfxP structural genes were found to be plasmid-coded. Our results extend the list of carboxydotrophy structural genes residing on the plasmid pHCG3 and strongly support the idea that the components essential for the chemolithoautotrophic utilization of CO by Pseudomonas carboxydovorans OM5 are plasmid-coded. A cfxL gene probe from Rhodospirillum rubrum did not detectably hybridize with DNA from any of the carboxydotrophic bacteria examined.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00245342
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  • 5
    Electronic Resource
    Electronic Resource
    The structural genes encoding CO dehydrogenase subunits (cox L, M and S) in Pseudomonas carboxydovorans OM5 reside on plasmid pHCG3 and are, with the exception of Streptomyces thermoautotrophicus, conserved in carboxydotrophic bacteria (1992)
    Springer
    Archives of microbiology 157 (1992), S. 301-304 
    Details
    ISSN: 1432-072X
    Keywords: Carbon monoxide ; CO ; Carboxydotrophic bacteria ; Plasmids ; CO Dehydrogenase ; Deoxyoligonucleotides ; Cox ; Pseudomonas carboxydovorans ; Pseudomonas carboxydohydrogena ; Pseudomonas carboxydoflava ; Streptomyces thermoautotrophicus ; Pseudomonas thermocarboxydovorans ; Bacillus schlegelii ; Alcaligenes carboxydus ; Arthrobacter ; Azomonas
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Employing deoxyoligonucleotide probes and Southern hybridizations, we have examined in carboxydotrophic bacteria the localization on the genome of genes encoding the large, medium and small subunits of CO dehydrogenase (coxL, M and S, respectively). In Pseudomonas carboxydovorans OM5 coxL, M and S were identified on the plasmid pHCG3; they were absent on the chromosome. This was evident from positive hybridizations with plasmid DNA of the wild-type strain OM5 and the absence of hybridizations with chromosomal DNA from the plasmid cured mutant strain OM5–12. The genes coxL, M and S were found on plasmids in all other plasmid-containing carboxydotrophic bacteria e.g. Alcaligenes carboxydus, Azomonas B1, Pseudomonas carboxydoflava, Pseudomonas carboxydovorans OM2 and OM4. Cox L, M and S could be identified on the chromosome of the plasmid-free bacteria Arthrobacter 11/x, Bacillus schlegelii, Pseudomonas carboxydohydrogena, and Pseudomonas carboxydovorans OM3. These results essentially confirm and extend former reports that cox genes are rather conserved among carboxydotrophic bacteria of distinct taxonomic position. However, Streptomyces thermoautotrophicus is an noteworthy exception since none of the three cox genes could be detected. This refers to a new type of CO dehydrogenase and is in accord with results indicating that the S. thermoautotrophicus CO dehydrogenase has an unusual electron acceptor specificity and some other properties setting it apart from the ‘classical’ CO dehydrogenases.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00245166
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  • 6
    Electronic Resource
    Electronic Resource
    Two proton high-spin excitations and dipole bands in192Hg (1994)
    Springer
    The European physical journal 348 (1994), S. 87-93 
    Details
    ISSN: 1434-601X
    Keywords: 27.80.+w ; 21.10.Hw ; 21.60.Ev
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract The192Hg nucleus was populated in the160Gd(36S, 4n) reaction at a beam energy of E=159 MeV. Emittedγ-rays were detected with the EUROGAM array comprising 43 Compton-suppressed large volume Ge detectors. The level scheme of192Hg has been extended up to an excitation energy of E=10.4 MeV and spin I=34 ħ. Two new structures, made of competing ΔI=1 and ΔI=2 transitions have been observed and their connexions with the low-lying levels established. Their lowest levels are located at 6.304 MeV and 6.879 MeV excitation energy. The experimental results are compared with mean-field HF+BCS calculations. It is proposed that the new structures originate from deformation-aligned quasi-proton excitations π(i13/2 * h9/2)K=11 andπ (h9/2) K=8 2 , coupled to rotation-aligned quasi-neutron ν(i13/2)n and quasi-proton π(h11/2)2 excitations.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01289594
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