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  • 1
    ISSN: 1432-072X
    Keywords: Klebsiella pneumoniae ; Nitrogen fixation ; Regulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The nifL gene product of Klebsiella pneumoniae inhibits the activity of the positive activator protein NifA in response to increased levels either of fixed nitrogen or of oxygen in the medium. In order to demonstrate that the responses to these two effectors are discrete we have subjected nifL to hydroxylamine mutagenesis and isolated nifL mutants that are impaired in their ability to respond to oxygen but not to fixed nitrogen. Two such mutations were sequenced and shown to be single base pair changes located in different parts of nifL. The amino acid sequence of NifL shows limited homology to the histidine protein kinases which comprise the sensing component of bacterial two-component regulatory systems. In the light of the location of one of the oxygen-insensitive mutations (Leu294Phe) we have reassessed this homology and we suggest that the Gln273-Leu317 region of NifL may facilitate interactions between NifL and NifA.
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  • 2
    ISSN: 1432-072X
    Keywords: Regulation ; ACV synthetase activity ; Glucose ; Glyceraldehyde-3-phosphate ; ATP ; l-cysteine ; β-Lactams ; Cephalosporium acremonium ; Streptomyces clavuligerus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The activity of δ-l-α-aminoadipyl)-l-cysteinyl-d-valine catalysis. Addition of l-cysteine to fermentation media increased β-lactam production in both organisms and alleviated the negative carbon source regulation by glycerol in S. clavuligerus.
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  • 3
    ISSN: 1432-072X
    Keywords: Key words     Methanosarcina barkeri ; Hydrogenase ; Regulation ; ATP synthesis ; Ferredoxin ; F420
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract      Acetate-grown cells of Methanosarcina barkeri MS were found to form methane from H2 : CO2 at the same rate as hydrogen-grown cells. Cells grown on acetate had similar levels of soluble F420-reactive hydrogenase I, and higher levels of cytochrome-linked hydrogenase II compared to hydrogen-grown cells. The hydrogenase I and II activities in the crude extract of acetate-grown cells were separated by differential binding properties to an immobilized Cu2+ column. Hydrogenase II did not react with ferredoxin or F420, whereas hydrogenase I coupled to both ferredoxin and F420. A reconstituted soluble protein system composed of purified CO dehydrogenase, F420-reactive hydrogenase I fraction, and ferredoxin produced H2 from CO oxidation at a rate of 2.5 nmol/ min · mg protein. Membrane-bound hydrogenase II coupled H2 consumption to the reduction of CoM-S-S-HTP and the synthesis of ATP. The differential function of hydrogenase I and II is ascribed to ferredoxin-linked hydrogen production from CO and cytochrome b-linked H2 consumption coupled to methanogenesis and ATP synthesis, respectively.
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  • 4
    ISSN: 1432-072X
    Keywords: Methanosarcina barkeri ; Hydrogenase ; Regulation ; ATP synthesis ; Ferredoxin ; F420
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Acetate-grown cells of Methanosarcina barkeri MS were found to form methane from H2:CO2 at the same rate as hydrogen-grown cells. Cells grown on acetate had similar levels of soluble F420-reactive hydrogenase I, and higher levels of cytochrome-linked hydrogenase II compared to hydrogen-grown cells. The hydrogenase I and II activities in the crude extract of acetate-grown cells were separated by differential binding properties to an immobilized Cu2+ column. Hydrogenase II did not react with ferredoxin or F420, whereas hydrogenase I coupled to both ferredoxin and F420. A reconstituted soluble protein system composed of purified CO dehydrogenase, F420-reactive hydrogenase I fraction, and ferredoxin produced H2 from CO oxidation at a rate of 2.5 nmol/min · mg protein. Membrane-bound hydrogenase II coupled H2 consumption to the reduction of CoM-S-S-HTP and the synthesis of ATP. The differential function of hydrogenase I and II is ascribed to ferredoxin-linked hydrogen production from CO and cytochrome b-linked H2 consumption coupled to methanogenesis and ATP synthesis, respectively.
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  • 5
    ISSN: 1432-072X
    Keywords: Nocardia sp. 239 ; Mixed substrates ; Methanol ; Formaldehyde ; Methylotrophy ; Regulation ; Continuous culture ; RuMP cycle ; l-Phenylalanine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The regulation of methanol metabolism in Nocardia sp. 239 was investigated. Growth on mixtures of glucose or acetate plus methanol in batch cultures resulted in simultaneous utilization of the substrates. The presence of glucose, but not of acetate, repressed synthesis of the ribulose monophosphate (RuMP) cycle enzymes hexulose-6-phosphate synthase (HPS) and hexulose-6-phosphate isomerase (HPI), and methanol was used as an energy source only. Comparable results were obtained following addition of formaldehyde (fed-batch system) to a culture growing on glucose. The synthesis of the methanol dissimilatory and assimilatory enzymes in Nocardia sp. 239 thus appears to be controlled differently. Methanol and/or formaldehyde induce the synthesis of these enzymes, but under carbon-excess conditions their inducing effect on HPS and HPI synthesis is completely overruled by glucose, or metabolites derived from it. Repression of the synthesis of these RuMP cycle enzymes was of minor importance under carbon- and energy-limiting conditions in chemostat cultures. Addition of a pulse of glucose to a formaldehyde-limited (2.5 mmol l−1 h−1) fed-batch culture resulted in a decrease in the levels of several enzymes of methanol metabolism (including HPI), whereas the HPS levels remained relatively constant. Increasing HPS/HPI activity ratios were also observed with increasing growth rates in formaldehyde-limited chemostat cultures. The data indicate that additional mechanisms, the identity of which remains to be elucidated, are involved in controlling the levels of these C1-specific enzymes in Nocardia sp. 239.
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  • 6
    ISSN: 1432-072X
    Keywords: Xanthobacter ; Taxonomy ; Methylotrophs ; Methanol ; Calvin cycle ; Carbon dioxide fixation ; RuBisC/O ; Regulation ; Continuous culture
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract All Xanthobacter strains studied are versatile autotrophic bacteria, able to grow on methanol and other substrates. Strain 25a, a yellow-pigmented, pleomorphic, Gram-negative bacterium, capable of autotrophic growth on methanol, formate, thiosulfate, and molecular hydrogen, was isolated from an enrichment culture inoculated with soil from a subtropical greenhouse. Subsequent studies showed that the organism also grows on a wide range of multicarbon substrates. Ammonia, nitrate and molecular nitrogen were used as nitrogen sources. The taxonomic relationship of strains H4-14 and 25a with previously described Xanthobacter strains was studied by numerical classification. Strain H4-14 was identified as a X. flavus strain, but the precise position of strain 25a remained uncertain. It probably belongs to a new species of the genus Xanthobacter. The levels of various enzymes involved in autotrophic and heterotrophic metabolism were determined following growth of strains H4-14 and 25a in batch and continuous cultures. The mechanisms involved in controlling ribulose-1,5-bisphosphate carboxylase/oxygenase synthesis in Xanthobacter strains appear to be comparable to those observed for other autotrophic bacteria, namely repression by organic compounds and derepression by autotrophic energy sources, such as methanol and hydrogen.
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  • 7
    ISSN: 1432-072X
    Keywords: Xanthobacter ; Methanol ; Formate ; Methylotrophy ; Autotrophy ; Calvin cycle ; Regulation ; Continuous culture ; RuBisC/O ; Carbon dioxide fixation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The regulation of C1-metabolism in Xanthobacter strain 25a was studied during growth of the organism on acetate, formate and methanol in chemostat cultures. No activity of methanol dehydrogenase (MDH), formate dehydrogenase (FDS) or ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisC/O) could be detected in cells grown on acetate alone over a range of dilution rates tested. Addition of methanol or formate to the feed resulted in the immediate induction of MDH and FDH and complete utilization (D=0.10 h-1) of acetate and the C 1-substrates. The activities of these enzymes rapidly dropped at the higher growth rates, which suggests that their synthesis is further controlled via repression by “heterotrophic” substrates such as acetate. Synthesis of RuBisC/O already occurred at low methanol concentrations in the feed, resulting in additive growth yields on acetate/methanol mixtures. The energy generated in the oxidation of formate initially allowed an increased assimilation of acetate (and a decreased dissimilation), resulting in enhanced growth yields on the mixture. RuBisC/O activity could only be detected at the higher formate/acetate ratios in the feed. The data suggest that synthesis of RuBisC/O and CO2 fixation via the Calvin cycle in Xanthobacter strain 25 a is controlled via a (de)repression mechanism, as is the case in other facultatively autotrophic bacteria. Autotrophic CO2 fixation only occurs under conditions with a diminished supply of “heterotrophic” carbon sources and a sufficiently high availability of suitable energy sources. The latter point is further supported by the clearly more pronounced derepressing effect exerted by methanol compared to formate.
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