ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
Filter
  • Carboxydotrophic bacteria  (3)
  • Zymomonas mobilis  (3)
  • Springer  (6)
  • Blackwell Publishing Ltd
  • Nature Publishing Group
  • Oxford University Press
  • 1990-1994  (6)
  • 1960-1964
  • 1950-1954
Collection
Keywords
Publisher
  • Springer  (6)
  • Blackwell Publishing Ltd
  • Nature Publishing Group
  • Oxford University Press
Years
Year
  • 1
    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
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Electron transport chain of Zymomonas mobilis (1990)
    Springer
    Archives of microbiology 154 (1990), S. 536-543 
    Details
    ISSN: 1432-072X
    Keywords: Zymomonas mobilis ; Glucose dehydrogenase ; Pyrroloquinoline quinone ; Ubiquinone ; Electron transport chain ; TMPD oxidase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The interaction of the membrane-bound glucose dehydrogenase from the anaerobic but aerotolerant bacterium Zymomonas mobilis with components of the electron transport chain has been studied. Cytoplasmic membranes showed reduction of oxygen to water with the substrates glucose or NADH. The effects of the respiratory chain inhibitors piericidin, capsaicin, rotenone, antimycin, myxothiazol, HQNO, and stigmatellin on the oxygen comsumption rates in the presence of NADH or glucose as substrates indicated that a complete and in the most parts identical respiratory chain is participating in the glucose as well as in the NADH oxidation. Furthermore, the presence of coenzyme Q10 (ubiquinone 10) in Z. mobilis was demonstrated. Extraction from and reincorporation of the quinone into the membranes revealed that ubiquinone is essential for the respiratory activity with glucose and NADH. In addition, a membrane-associated tetramethyl-p-phenylene-diamine-oxidase activity could be detected in Z. mobilis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00248833
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Formation of acetyl-CoA in Zymomonas mobilis by a pyruvate dehydrogenase complex (1993)
    Springer
    Archives of microbiology 159 (1993), S. 197-199 
    Details
    ISSN: 1432-072X
    Keywords: Zymomonas mobilis ; Pyruvate dehydrogenase multienzyme complex ; Anaerobic formation of acetyl-CoA
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In the gram negative, obligately ethanologenic bacterium Zymomonas mobilis a pyruvate dehydrogenase complex was identified and the complex was enriched from cell extracts. This multienzyme complex is responsible for acetyl-CoA biosynthesis from pyruvate. No activities of related multienzyme complexes, 2-ketoglutarate dehydrogenase and branched chain keto acid dehydrogenase, could be detected.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00250282
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 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
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 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
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 6
    Electronic Resource
    Electronic Resource
    Oxidative phosphorylation in Zymomonas mobilis (1993)
    Springer
    Archives of microbiology 160 (1993), S. 74-79 
    Details
    ISSN: 1432-072X
    Keywords: Zymomonas mobilis ; Oxidative phosphorylation ; membrane vesicles ; ATP synthesis ; transmembrane pH gradient ; 31P-NMR ; Acetaldehyde ; Ethanol metabolism
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The obligately fermentative aerotolerant bacterium Zymomonas mobilis was shown to possess oxidative phosphorylation activity. Increased intracellular ATP levels were observed in aerated starved cell suspension in the presence of ethanol or acetaldehyde. Ethanolconsuming Z. mobilis generated a transmembrane pH gradient. ATP synthesis in starved Z. mobilis cells could be induced by external medium acidification of 3.5–4.0 pH units. Membrane vesicles of Z. mobilis coupled ATP synthesis to NADH oxidation. ATP synthesis was sensitive to the protonophoric uncoupler CCCP both in starved cells and in membrane vesicles. The H+-ATPase inhibitor DCCD was shown to inhibit the NADH-coupled ATP synthesis in membrane vesicles. The physiological role of oxidative phosphorylation in this obligately fermentative bacterium is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00258148
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...