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  • 1
    Call number: AWI Bio-99-0367
    In: Biotechnology handbooks
    Type of Medium: Monograph available for loan
    Pages: XIV, 286 S. : graph. Darst.
    ISBN: 030643878X
    Series Statement: Biotechnology handbooks 5
    Branch Library: AWI Library
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 136 (1983), S. 219-221 
    ISSN: 1432-072X
    Keywords: Xanthobacter ; Nitrogen fixation ; Oxygen sensitivity ; Nitrogen metabolism ; Glutamine synthetase ; Glutamate synthase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract N2-fixation was investigated in the chemoautotrophic hydrogen bacterium Xanthobacter H4-14. N2-fixing batch cultures of this organism could only be grown at pO2 values of around 0.02 bar, and in continuous culture dissolved oxygen tensions above 16 μM were found to inhibit N2-fixation. Xanthobacter H4-14 utilized a variety of amino acids, nitrate and ammonia as nitrogen sources. Cell-free extracts from steady-state continuous cultures of ammonia grown, nitrate grown and N2-fixing Xanthobacter were assayed for the presence of ammonia assimilation enzymes. No alanine dehydrogenase or glutamate dehydrogenase activity was detected. Ammonia was assimilated exclusively via the glutamine synthetase/glutamate synthase pathway, irrespective of the extracellular concentration of ammonia.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1432-072X
    Keywords: Methanotroph ; Methane oxidation ; Methane monooxygenase ; Oligonucleotide probing ; Subunit genes ; Methylococcus capsulatus (Bath)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Methane monooxygenase (MMO) is the enzyme responsible for the conversion of methane to methanol in methanotrophic bacteria. In addition, this enzyme complex oxidizes a wide range of aliphatic and aromatic compounds in a number of potentially useful biotransformations. In this study, we have used biochemical data obtained from purification and characterization of the soluble MMO from Methylococcus capsulatus (Bath), to identify structural genes encoding this enzyme by oligonucleotide probing. The genes encoding the β and γ subunits of MMO were found to be chromosomally located and were linked in this organism. We report here on the analysis of a recombinant plasmid containing 12 kilobases of Methylococcus DNA and provide the first evidence for the localization and linkage of genes encoding the methane monooxygenase enzyme complex. DNA sequence analysis suggests that the primary structures of the β and γ subunit of MMO are completely novel and the complete sequence of these genes is presented.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1432-072X
    Keywords: Rhodococcus ; Propane metabolism ; Alcohol dehydrogenase ; Mutagenesis ; Terminal oxidation ; Sub-terminal oxidation ; Western-blotting
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract NAD+-dependent propan-1-ol and propan-2-ol dehydrogenase activities were detected in cell-free extracts of Rhodococcus rhodochrous PNKb1 grown on propane and potential intermediates of propane oxidation. However, it was unclear whether this activity was mediated by one or more enzymes. The isolation of mutants unable to utilize propan-1-ol (alcA-) or propan-2-ol (alcB-) as sole carbon and energy sources demonstrated that these substrates are metabolized by different alcohol dehydrogenases. These mutants were also unable to utilize propane as a growth substrate indicating that both alcohols are intermediates of propane metabolism. Therefore, propane is metabolized by terminal and sub-terminal oxidation pathways. Westernblot analysis demonstrated that a previously purified NAD+-dependent propan-2-ol dehydrogenase (Ashraf and Murrell 1990) was only synthesized after growth on propane and sub-terminal oxidation intermediates (but not acetone), and not propan-1-ol or terminal oxidation intermediates. Therefore, our evidence suggest that another dehydrogenase is involved in the metabolism of propan-1-ol and this agrees with the isolation of the alcA- and alcB- phenotypes. The previously characterized NAD+-dependent propan-2-ol dehydrogenase from R. rhodochrous PNKb1 is highly conserved amongst members of the propane-utilizing Rhodococcus-Nocardia complex.
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1432-072X
    Keywords: Key wordsThiobacillus taxonomy ; Thiobacillus ; aquaesulis ; Thiobacillus halophilus ; 16S rRNA ; phylogeny ; 16S rDNA sequences ; Proteobacteria
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Total base sequences of the 16S rRNA genes of Thiobacillus halophilus and Thiobacillus aquaesulis show that these bacteria fall into the gamma- and beta-subdivisions, respectively of the Proteobacteria. The closest relative of T. halophilus is Thiobacillus hydrothermalis (with 98.7% similarity), and the closest relative of T. aquaesulis is Thiobacillus thioparus (93.2% similarity). Physiological properties and mol% G+C content of their DNA serve to confirm that these four organisms are all distinct species. It is reiterated that the species currently assigned to the genus Thiobacillus are clearly so diverse that they need reclassification into several genera. The type species, T. thioparus, is unequivocally placed in the beta-subdivision of the Proteobacteria, thus requiring that the use of the genus name Thiobacillus be restricted to the chemolithoautotrophic species falling into that group. T. aquaesulis and T. thioparus may thus be regarded as true species of Thiobacillus. The relatively large number of obligately chemolithoautotrophic Thiobacillus species falling in the gamma-subdivision of the Proteobacteria need further study in order to assess the case for reclassification into one or more new or different genera.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 173 (2000), S. 325-332 
    ISSN: 1432-072X
    Keywords: Methanotroph Methane oxidation Methane monooxygenase genes Regulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract. Methanotrophs are ubiquitous in the environment and play an important role in mitigating global warming due to methane. They are also potentially interesting for industrial applications such as production of bulk chemicals or bioremediation. The first step in the oxidation of methane is the conversion to methanol by methane monooxygenase, the key enzyme, which exists in two forms: the cytoplasmic, soluble methane monooxygenase (sMMO) and the membrane-bound, particulate methane monooxygenase (pMMO). This paper reviews the biochemistry and molecular biology of both forms of MMO. In the past few years there have been many exciting new findings. sMMO components have been expressed in heterologous and homologous hosts. The pMMO has been purified and biochemically studied in some detail and the genes encoding the pMMO have been sequenced. Copper ions have been shown to play a key role in regulating the expression of both MMO enzyme complexes. We also present a model for copper regulation based on results from Northern analysis, primer-extensions and new sequence data, and raise a number of unanswered questions for future studies.
    Type of Medium: Electronic Resource
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  • 7
    ISSN: 1432-072X
    Keywords: Rhodococcus ; Propane metabolism ; Secondary alcohol dehydrogenase ; Protein purification ; Terminal oxidation ; Sub-terminal oxidation ; NAD-agarose
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract NAD+-linked primary and secondary alcohol dehydrogenase activity was detected in cell-free extracts of propane-grown Rhodococcus rhodochrous PNKb1. One enzyme was purified to homogeneity using a two-step procedure involving DEAE-cellulose and NAD-agarose chromatography and this exhibited both primary and secondary NAD+-linked alcohol dehydrogenase activity. The Mr of the enzyme was approximately 86,000 with subunits of Mr 42,000. The enzyme exhibited broad substrate specificity, oxidizing a range of short-chain primary and secondary alcohols (C2−C8) and representative cyclic and aromatic alcohols. The pH optimum was 10. At pH 6.5, in the presence of NADH, the enzyme catalysed the reduction of ketones to alcohols. The K m values for propan-1-ol, propan-2-ol and NAD were 12 mM, 18 mM and 0.057 mM respectively. The enzyme was inhibited by metal-complexing agents and iodoacetate. The properties of this enzyme were compared with similar enzymes in the current literature, and were found to be significantly different from those thus far described. It is likely that this enzyme plays a major role in the assimilation of propane by R. rhodochrous PNKb1.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 157 (1991), S. 60-65 
    ISSN: 1432-072X
    Keywords: Marine methanotroph ; Methane oxidation ; Methylomonas ; Ammonia assimilation ; Nitrogen metabolism
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Two new methane-oxidizing bacteria have been isolated from seawater samples from Plymouth Sound. These marine methanotrophs have an obligate requirement for NaCl and exhibit many properties of typical Type I methanotrophs previously isolated from freshwater environments. However, they are different from all other methanotrophs thus far described in that they failed to grow on all solid media tested. The nitrogen metabolism of both strains was investigated. They were not N2-fixers nor would they use ammonia as nitrogen source. They appeared to utilize the glutamate dehydrogenase pathway for the assimilation of ammonia under all growth conditions tested.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 164 (1995), S. 294-300 
    ISSN: 1432-072X
    Keywords: Key words Acetylene reduction ; Nitrogen fixation ; Leptospirillum ferrooxidans ; Thiobacillus ferrooxidans
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Acetylene reduction was observed with ferrous-iron-oxidizing Thiobacillus ferrooxidans, as expected from previous studies with this bacterium. Acetylene reduction was also found during the growth of T. ferrooxidans on tetrathionate. Only Leptospirillum ferrooxidans, one of several other phylogenetically diverse, ferrous-iron- and/or sulfur-oxidizing acidophilic microorganisms, also reduced acetylene. A reduction of the oxygen concentration in the culture atmosphere was necessary to alleviate inhibition of nitrogenase activity. DNA sequences homologous to nif structural genes were found in both organisms. Diazotrophic growth of L. ferrooxidans was inferred from an increase in iron oxidation in ammonium-free medium when the oxygen concentration was limited and from apparent inhibition by acetylene under these conditions.
    Type of Medium: Electronic Resource
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  • 10
    ISSN: 1432-072X
    Keywords: Key wordsMethylosulfonomonas methylovora ; Marinosulfonomonas methylotropha ; Methanesulfonic ; acid ; 16S rRNA phylogeny ; 16S rDNA sequences ; Proteobacteria
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Two novel genera of restricted facultative methylotrophs are described; both Methylosulfonomonas and Marinosulfonomonas are unique in being able to grow on methanesulfonic acid as their sole source of carbon and energy. Five identical strains of Methylosulfonomonas were isolated from diverse soil samples in England and were shown to differ in their morphology, physiology, DNA base composition, molecular genetics, and 16S rDNA sequences from the two marine strains of Marinosulfonomonas, which were isolated from British coastal waters. The marine strains were almost indistinguishable from each other and are considered to be strains of one species. Type species of each genus have been identified and named Methylosulfonomonas methylovora (strain M2) and Marinosulfonomonas methylotropha (strain PSCH4). Phylogenetic analysis using 16S rDNA sequencing places both genera in the α-Proteobacteria. Methylosulfonomonas is a discrete lineage within the α-2 subgroup and is not related closely to any other known bacterial genus. The Marinosulfonomonas strains form a monophyletic cluster in the α-3 subgroup of the Proteobacteria with Roseobacter spp. and some other partially characterized marine bacteria, but they are distinct from these at the genus level. This work shows that the isolation of bacteria with a unique biochemical character, the ability to grow on methanesulfonic acid as energy and carbon substrate, has resulted in the identification of two novel genera of methylotrophs that are unrelated to any other extant methylotroph genera.
    Type of Medium: Electronic Resource
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