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  • 1
    Electronic Resource
    Electronic Resource
    Time-resolved measurement of G values of solute excited states in cyclohexane and n-hexane (1991)
    s.l. : American Chemical Society
    The @journal of physical chemistry 〈Washington, DC〉 95 (1991), S. 728-730 
    Details
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/j100155a044
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  • 2
    Electronic Resource
    Electronic Resource
    Pulse radiolysis studies of ion–electron recombination in helium. Pressure and temperature effects (1992)
    College Park, Md. : American Institute of Physics (AIP)
    The Journal of Chemical Physics 97 (1992), S. 1800-1808 
    Details
    ISSN: 1089-7690
    Source: AIP Digital Archive
    Topics: Physics , Chemistry and Pharmacology
    Notes: Using pulse radiolysis techniques, rates of recombination of electrons with He+2 ions in the presence of helium over a wide pressure range (40–900 Torr) and at temperatures of 200, 235, 275, and 295 K were measured. Two- and three-body recombination processes were resolved, and a temperature dependence for the three-body recombination rate constant of T(−2.9±1.2)gas observed. This result agrees well with theoretical predictions of a temperature exponent of −2.5 by Bates and Khare and Pitaevskii, and remarkably well with recent work by Cao and Johnsen which gave a temperature exponent of −2.9 for the rate constant for three-body recombination of electrons with simple molecular ions in the presence of helium.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.463167
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  • 3
    Electronic Resource
    Electronic Resource
    A temperature effect in the luminescence emission from electron-irradiated MgO (1990)
    College Park, Md. : American Institute of Physics (AIP)
    The Journal of Chemical Physics 92 (1990), S. 6441-6446 
    Details
    ISSN: 1089-7690
    Source: AIP Digital Archive
    Topics: Physics , Chemistry and Pharmacology
    Notes: The temperature dependence of luminescence emissions from electron-irradiated CaO and MgO single crystals has been studied by time resolved luminescence spectroscopy after pulsed nanosecond irradiation with 0.20 to 0.60 MeV electrons. Emissions from CaO at 375 nm at both 293 and 83 K, show similar threshold characteristics for atomic displacement. These have been attributed to the displacement of oxygen ions and subsequent electron trapping, resulting in the formation of F+ centers. The threshold energy of 0.32±0.01 MeV corresponds to an oxygen displacement energy of 58±2 eV. A 380 nm emission from MgO, also attributed to oxygen displacement and F+ center formation, shows no temperature effect, with a displacement threshold virtually identical to that for CaO. A 235 nm emission from MgO shows a significant temperature effect. The threshold energy at 293 K is 0.31±0.01 MeV, whilst at 83 K two thresholds are observed, 0.31±0.01 and 0.41±0.01 MeV.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.458596
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  • 4
    Electronic Resource
    Electronic Resource
    Pulse radiolysis studies of ion-electron recombination in gaseous argon (1993)
    College Park, Md. : American Institute of Physics (AIP)
    The Journal of Chemical Physics 98 (1993), S. 383-389 
    Details
    ISSN: 1089-7690
    Source: AIP Digital Archive
    Topics: Physics , Chemistry and Pharmacology
    Notes: Using pulse radiolysis techniques, rates of recombination of Ar2+ ions with electrons in bulk argon were measured over a wide pressure range (150 to 1065 torr) at bulk gas temperatures of 295, 335, and 375 K. No pressure dependence for the total recombination rate constant was observed at any temperature studied. This observation is consistent with the model, whereby the encounter pair is stabilized by electron energy loss while in the Coulomb field of the cation. The presence of a Ramsauer minimum in the electron/argon atom momentum-transfer cross section versus energy profile means that, at low energies, energy loss is very slow. The neutral-assisted three-body recombination mechanism in argon does not significantly enhance the total rate of recombination above the two-body rate.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.464631
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  • 5
    Electronic Resource
    Electronic Resource
    Measurement of krypton dimer(+)/chloride ionic recombination rate constants in krypton (1992)
    s.l. : American Chemical Society
    The @journal of physical chemistry 〈Washington, DC〉 96 (1992), S. 8858-8863 
    Details
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/j100201a033
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  • 6
    Electronic Resource
    Electronic Resource
    Ion recombination rates in rare gas cation-halide anion systems. 3. Xenon bromide (XeBr*) and xenone iodide (XeI*) (1993)
    s.l. : American Chemical Society
    The @journal of physical chemistry 〈Washington, DC〉 97 (1993), S. 9413-9419 
    Details
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/j100139a027
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  • 7
    Electronic Resource
    Electronic Resource
    Ion recombination rates in rare-gas cation-halide anion systems. 2. Krypton fluoride and xenon chloride eximers (1991)
    s.l. : American Chemical Society
    The @journal of physical chemistry 〈Washington, DC〉 95 (1991), S. 3152-3158 
    Details
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/j100161a037
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  • 8
    Electronic Resource
    Electronic Resource
    Stimulation of phosphorylation and inactivation of pyruvate dehydrogenase by physiological inhibitors of the pyruvate dehydrogenase reaction (1975)
    [s.l.] : Nature Publishing Group
    Nature 257 (1975), S. 808-809 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Mammalian pyruvate dehydrogenases contain three enzymes, pyruvate decarboxylase (Ei), dihydrolipoate acetyltransferase (£.〉) and dihydrolipoyl dehydrogenase (E:!) bound together in a single complex. They catalyse the conversion of pyruvate, CoA and NAD into acetyl CoA, NADH〉 and CO-2 in ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/257808a0
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  • 9
    Electronic Resource
    Electronic Resource
    The utilisation of d-galactonate and d-2-oxo-3-deoxygalactonate by Escherichia coli K-12 (1978)
    Springer
    Archives of microbiology 118 (1978), S. 199-206 
    Details
    ISSN: 1432-072X
    Keywords: E. coli K-12 ; Galactonate ; 2-Oxo-3-deoxygalactonate ; Genetic mapping
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract 1. Escherichia coli K-12 mutants unable to grow on d-galactonate have been isolated and found to be defective in either galactonate dehydratase, 2-oxo-3-deoxygalactonate 6-phosphate aldolase or devoid of both of these enzymes and of 2-oxo-3-deoxygalactonate kinase. 2. 2-Oxo-3-deoxygalactonate kinase and 2-oxo-3-deoxygalactonate 6-phosphate aldolase are still induced by galactonate in mutants lacking galactonate dehydratase, suggesting that galactonate rather than a catabolic product of galactonate is the inducer of the galactonate catabolic enzymes. Synthesis of the enzymes is subject to glucose catabolite repression. 3. Mutants defective in 2-oxo-3-deoxygalactonate 6-phosphate aldolase accumulate 2-oxo-3-deoxygalactonate 6-phosphate when exposed to galactonate and this compound causes general growth inhibition. 4. Secondary mutants that no longer show this inhibition fail to make 2-oxo-3-deoxygalactonate 6-phosphate due to additional defects in galactonate transport, galactonate dehydratase, 2-oxo-3-deoxygalactonate kinase or a putative promoter mutation that prevents formation of these enzymes. 5. A spontaneous mutant capable of growth on 2-oxo-3-deoxygalactonate has been isolated. It has two genetically distinct mutations. One permits constitutive formation of the galactonate catabolic enzymes and the other allows the uptake of 2-oxo-3-deoxygalactonate. Neither mutation on its own permitted growth on 2-oxo-3-deoxygalactonate. 6. Genes specifying the various galactonate catabolic enzymes have been located at min 81.7 on the E. coli K-12 linkage map and probably constitute an operon. The gene sequence in this region was shown to by: pyrE uhp dgo dnaA.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00415730
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  • 10
    Electronic Resource
    Electronic Resource
    Catabolism of 3-hydroxybenzoate by the gentisate pathway in Klebsiella pneumoniae M5a1 (1990)
    Springer
    Archives of microbiology 154 (1990), S. 489-495 
    Details
    ISSN: 1432-072X
    Keywords: Klebsiella pneumoniae M5a1 ; 3-Hydroxybenzoate degradation ; Gentisate pathway ; 3-Hydroxybenzoate monooxygenase mutants ; Maleylpyruvate isomerase mutants
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Growth of Klebsiella pneumoniae M5a1 on 3-hydroxybenzoate leads to the induction of 3-hydroxybenzoate monooxygenase, 2,5-dihydroxybenzoate dioxygenase, maleylpyruvate isomerase and fumarylpyruvate hydrolase. Growth in the presence of 2,5-dihydroxybenzoate also induces all of these enzymes including the 3-hydroxybenzoate monooxygenase which is not required for 2,5-dihydroxybenzoate catabolism. Mutants defective in 3-hydroxybenzoate monooxygenase fail to grow on 3-hydroxybenzoate but grow normally on 2,5-dihydroxybenzoate. Mutants lacking maleylpyruvate isomerase fail to grow on 3-hydroxybenzoate and 2,5-dihydroxybenzoate. Both kinds of mutants grow normally on 3,4-dihydroxybenzoate. Mutants defective in maleylpyruvate isomerase accumulate maleylpyruvate when exposed to 3-hydroxybenzoate and growth is inhibited. Secondary mutants that have additionally lost 3-hydroxybenzoate monooxygenase are no longer inhibited by the presence of 3-hydroxybenzoate. The 3-hydroxybenzoate monooxygenase gene (mhbM) and the maleylpyruvate isomerase gene (mhbI) are 100% co-transducible by P1 phage.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00245233
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