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  • Respiratory chains  (2)
  • 36.10.DR  (1)
  • Springer  (3)
  • Springer Nature
  • 2020-2022
  • 1985-1989  (3)
  • 1950-1954
Sammlung
Verlag/Herausgeber
  • Springer  (3)
  • Springer Nature
Erscheinungszeitraum
  • 2020-2022
  • 1985-1989  (3)
  • 1950-1954
Jahr
  • 1
    ISSN: 1432-072X
    Schlagwort(e): Iron-limitation ; Escherichia coli ; Respiratory chains ; Cytochromes ; Gallium ; Metal uptake
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract The effects of iron limitation on growth, the composition and function of the respiratory chains, and gallium uptake inEscherichia coli have been studied. Decreasing the iron concentration in a defined medium using Chelex resin gave lower growth yields in both continuous culture and prolonged batch culture. In the former, ironlimited (entering [Fe]≤2.0 μM) cells exhibited diminished respiration rates, respiration-driven proton translocation quotients, and levels of non-haem iron and cytochromes. The cellular concentration of haemoproteinb-590 (a cytochromea 1-like hydroperoxidase) decreased 20-fold on iron limitation, whilst a CO-binding pigment with an absorption maximum in the dithionite-treated form near 500 nm appeared. Gallium(III) (9 μM) added to iron-limited, but not iron-sufficient, cultures diminished growth yields further; cells grown with low entering concentrations of iron took up less gallium than iron-sufficient cells. These results are attributed to the interference by gallium(III) with siderophore-mediated metal uptake. Gallium also stimulated iron uptake and was itself accumulated by iron-sufficient cells, suggesting that gallium(III) also affects the iron transport system(s) of low affinity.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 2
    ISSN: 1432-072X
    Schlagwort(e): Copper-limitation ; Escherichia coli ; Cytochrome oxidases ; Oxygen reduction ; Respiratory chains
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract The role(s) of copper in a bacterial cytochrome oxidase of the aa 3-type was investigated by growth of Paracoccus denitrificans NCIB 8944, in batch and steady state continuous culture, in a medium from which the bulk of the copper had been extracted. In a medium containing approximately 0.02 μM copper, cellular copper content, cytochromes a+a 3 and cytochrome a 3 were reduced to 55%, 58% and 33% respectively of control values and there were also less marked decreases in cytochromes c+c 1 (to 85%) and a CO-binding b-type cytochrome, possibly cytochrome o (to 71%). Copper deficiency elicited in reduced minus oxidized difference spectra a shift to shorter wavelengths and narrowing of the band width of the α-band of the oxidase, and loss of a (negative) band near 830 nm attributable to CuA (the copper functionally associated with haem a in the oxidase complex). The oxidase in copper-deficient cells reacted with oxygen to form the oxy “Compound A” at rates similar to that in control cells but CO recombination to ferrous haem a 3 was slowed 4-fold in the copper deficient case. The results are interpreted as indicating loss of CuA and changes in the proportions of haems a and a 3 with retention of catalytic activity. Titrations of respiration rates with antimycin suggested that copper deficiency did not result in diversion of electron flux through an antimycin A-insensitive, cytochrome o-terminated branch of the respiratory chain.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 3
    ISSN: 1434-6079
    Schlagwort(e): 36.10.DR
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Physik
    Notizen: Abstract We report the first measurement of the polarization of thermal muonium in vacuum. A 20 MeV/c beam of μ+ was stopped in a layer of SiO2 powder which emitted (17±1)% of the stopped μ+ into vacuum as thermal muonium. The muonium Larmor precession was observed in a transverse magnetic field of 1.4 G, and the measured amplitude of the precession signal indicates that the μ+ polarization in the muonium is (39±9)%.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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