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  • Biochemistry and Biotechnology  (4)
  • Induction  (2)
  • d-Ribulose 1,5-diphosphate carboxylase  (2)
  • 1
    ISSN: 1432-072X
    Keywords: d-Ribulose 1,5-diphosphate carboxylase ; Oxygenase activity ; Quaternary structure ; Electron microscopy ; Alcaligenes eutrophus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract d-Ribulose 1,5-diphosphate carboxylase has been purified from autotrophically grown cells of the facultative chemolithotrophic hydrogen bacteriumAlcaligenes eutrophus. The enzyme was homogeneous by the criteria of polyacrylamide gel electrophoresis. The molecular weight of the enzyme was 505000 determined by gel filtration and sucrose density gradient centrifugation, and a sedimentation coefficient of 18.2 S was obtained. It was demonstrated by sodium dodecyl sulphate-polyacrylamide gel electrophoresis that the enzyme consists of two types of subunits of molecular weight 52000 and 13000. Electron microscopy on the intact and the partially dissociated enzyme lead to the construction of a model for the quaternary structure of the enzyme which is composed of 8 large and 8 small subunits. The most probable symmetry of the enzyme molecule is 4:2:2. Michaelis constant (K m ) values for ribulose 1,5-diphosphate, Mg2-, and CO2 were 0.59 mM, 0.33 mM, and 0.066 mM measured under air. Oxygen was a competitive inhibitor with respect to CO2 suggesting that the enzyme also exhibits an oxygenase activity. The oxygenolytic cleavage of ribulose 1,5-diphosphate was shown and a 1:1 stoichiometry between oxygen consumption and 3-phosphoglycerate formation observed.
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  • 2
    ISSN: 1432-072X
    Keywords: Glycollate excretion ; Phosphoglycol-late phosphatase ; Glycollate oxidoreductase ; d-Ribulose 1,5-diphosphate carboxylase ; Alcaligenes eutrophus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Autotrophic cultures of the facultative chemolithotrophAlcaligenes eutrophus have been found to excrete glycollate. This excretion was greatly stimulated by the incorporation of up to 20% (v/v) oxygen in the hydrogen used for gassing. The stimulatory effect of oxygen was prevented by the addition of 10% (v/v) CO2 to the gassing mixture. Glycollate excretion only in the presence of oxygen was increased by the addition of 2-pyridyl-hydroxymethane sulphonic acid (HPMS), an inhibitor of glycollate oxidation, indicating that glycollate formation itself was stimulated by oxygen. No glycollate excretion by cultures grown heterotrophically on pyruvate was detected, either in the absence or presence of HPMS, under heterotrophic or autotrophic conditions. Extracts from autotrophic cells showed phosphoglycollate phosphatase and glycollate oxidoreductase activities, which were considerably lower in extracts prepared from pyruvate- or fructose-grown (heterotrophic) cells. The increase in activity of both enzymes upon cell transfer from heterotrophic to autotrophic growth was prevented by chloramphenicol and resembled the induction ofd0ribulose 1,5-diphosphate carboxylase under the same conditions.
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  • 3
    ISSN: 1432-072X
    Keywords: R-Bodies ; Kappa particles ; Free-living hydrogen bacteria ; Induction ; Electron microscopy ; Chemical composition ; Defective prophages ; Plasmids
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract R-Bodies have been found in a recently isolated pseudomonas-like free-living hydrogen oxidizing bacterium. Their isolation, fine structure and chemical composition are described and compared with the R-bodies from the kappa particles (Caedobacter), obligate endosymbionts of Paramecium aurelia. The 2K 1 R-bodies exhibited essential characteristics of the kappa R-bodies; however, their size and some other structural aspects proved that they represent a new type of R-bodies. The presence of phage tail-like particles in cells induced with Mitomycin C is in favour of the hypothesis that the R-bodies might be coded by defective prophages, or by extrachromosomal elements.
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  • 4
    ISSN: 1432-072X
    Keywords: Aquaspirillum autotrophicum ; Hydrogen bacterium ; Growth ; Chemolithoautotrophy ; Particulate hydrogenase ; Induction ; Repression ; Natural habitats
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Aquaspirillum autrotrophicum, an aerobic hydrogen bacterium recently isolated from an eutrophic freshwater lake, was characterized physiologically. It grew autotrophically in a fermenter with a doubling time of 4 h. Heterotrophic growth was faster. pH-Optimum ranged from 5.0–7.5, temperature optimum was about 28° C. During autotrophic growth about 10 moles hydrogen were consumed per 1 mole carbon dioxide fixed. Hydrogenase activity is inducible. CO2 did not enhance the oxy-hydrogen reaction by intact cells. The hydrogenase activity was localized in the particulate fraction. The hydrogenase reduced methylene blue and phenazine methosulfate; pyridine nucleotides were not reduced. In cell-free extracts, hydrogenase was sensitive to oxygen. Ribulosebisphosphate carboxylase was present in autotrophically-grown cells and absent from heterotrophically grown cells. Hydrogenase induction in heterotrophically-grown cells followed parabolic kinetics. Oxygen and D-gluconate repressed hydrogenase synthesis, whereas citrate, DL-lactate and pyruvate stimulated its formation. The repressive effect was delayed. The results suggest that the control of hydrogenase synthesis occurred at the transcriptional level, and that mRNA coding for the hydrogenase had a relatively long life span. D-Gluconate was degraded via the Entner-Doudoroff pathway, the enzymes of which were constitutively formed. Enzymes of the pentosephosphate and Embden-Meyerhof pathways (except phosphofructokinase) were present, too. Hydrogen did not inhibit heterotrophic growth. The possible competitive advantage of the physiological properties described with regard to the natural habitat was discussed.
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  • 5
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 22 (1980), S. 1895-1906 
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Empirical estimations of H2O2 concentration in a system containing bovine liver catalase and continually supplied with H2O2 were done to evaluate the efficiency of the enzyme to cleave H2O2. It was found that the continuous addition of H2O2 leads to the formation of steady-state concentrations of H2O2 in the medium. At a constant catalase concentration both the level and the duration of the steady state are dependent on the flow rate of H2O2. The increase of the catalase concentration in the medium does not change the steady-state level, it merely leads to the maintenance of the steady state for longer durations. At higher flow rates of H2O2, no steady state could be maintained, even when catalase was present in high excess. The incomplete cleavage of H2O2 by catalase under these conditions is due to the low affinity of catalase toward H2O2 (high Km value, apparent Km = 0.1M H2O2) and to the rapid inactivation of the enzyme during the continuous addition of H2O2.
    Additional Material: 6 Ill.
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  • 6
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 22 (1980), S. 1877-1894 
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The supply of heterotrophically growing suspensions of Alcaligenes eutrophus PHB-4 with oxygen formed by the continuous addition of H2O2 in the presence of bovine liver catalase was found to be restricted to well-defined conditions. The catalase-H2O2 system proved to be suitable during the growth at low cell densities equivalent to 2 g dry weight/liter. When under these conditions the oxygen concentration was held constant at 1.8 mg O2/liter, the cells grew for 6-8 hr at a rate almost identical to that observed with conventional aeration. However, aeration with H2O2 for longer durations (10-20 hr) and at higher cell densities (5-20 g dry weight/liter) led invariably to cell damage and retardation of growth. The impairment of growth observed during the oxygen supply by the catalase-H2O2 system was traced back to the formation of gradually increasing steady-state concentrations of H2O2 in the medium. Possible sites of cell damage by H2O2 such as membrane function, excretion and function of siderophores, and synthesis of cell polymers have been studied, and the cytotoxic mechanism of low concentrations of H2O2 was discussed.
    Additional Material: 9 Ill.
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  • 7
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A catalase has been purified from aerobically grown Escherichia coli K12. The enzyme exhibits unorthodox properties compared with catalyse from bovine liver and seems to be identical to hydroperoxidase II from E. coli. A mathematical model is presented which makes it possible to calculate the steady-state concentration of hydrogen peroxide in an open system. The model has been verified experimentally. It has been shown that the catalase from E. coli is better suited than the bovine liver enzyme for oxygen supply to cell suspensions using hydrogen peroxide.
    Additional Material: 1 Ill.
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  • 8
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 19 (1977), S. 413-424 
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Oxygen has been supplied to suspensions of microorganisms kept under nitrogen by the addition of hydrogen peroxide. If catalase was present in the suspension and the flow was adjusted to the rate of oxygen consumption, the cells grew at rates identical to the controls incubated under air. The applicability of oxygen supply by hydrogen peroxide and its limits are discussed.
    Additional Material: 6 Ill.
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