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  • 1
    ISSN: 1520-5126
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Journal of bioenergetics and biomembranes 12 (1980), S. 265-276 
    ISSN: 1573-6881
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract Spectra of oxidized and reduced cytochromed in particles ofA. vinelandii were studied in the presence of the ligands CO, azide, and NH2OH under oxidizing, reducing, and turnover conditions. Under oxidizing conditions, spectral changes were observed on oxidized cytochromed (absorption maximum at 648 nm) in the presence of CO and NH2OH showing a shift of the maximum to shorter wavelengths (639 and 645 nm, respectively) and a broadening of the half-band width. Under reducing conditions, spectral changes were observed on reduced cytochromed (absorption maximum at 631 nm) in the presence of CO (absorption maximum at 636 nm), NO, NO− 2, and NH2OH (absorption maximum at 642 nm in the presence of dithionite). The spectral changes of cytochromed in the presence of NH2OH or with dithionite and NO− 2 were ascribed to the formation of the NO-cytochromed compound. Under turnover conditions CO, NH2OH, and azide cause a spectral shift of the absorption maximum of cytochromed from 648 nm to 636, 645, and 655 nm, respectively. With NH2OH and azide a broadening of the half-band width of 7 and 6 nm, respectively, was also observed. The spectral changes caused by CO and NH2OH were interpreted as a binding of the ligands to cytochromed changing its conformation from the oxidized state absorbing at 648 nm into a more stable liganded form. Since azide does not affect the spectral bands of oxidized and reduced cytochromed, the spectral change during turnover in the presence of azide were ascribed to a preferential binding of azide to enzymically active conformation of cytochromed (cytochromed x).
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Journal of bioenergetics and biomembranes 7 (1975), S. 215-222 
    ISSN: 1573-6881
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract Oxidized particles ofA. vinelandii show high-spin ferric signals with an axial and a rhombically distorted component with g-values at 5.94 and 6.24, 5.51, respectively. The signals behave similarly on variation of temperature and/or power and are, assigned to cytochromed. The addition of ligands such as cyanide and carbon monoxide to oxidized particles mainly affects the rhombic component of the signal in the g=6 region. Prolonged, incubation of cyanide with oxidized particles results in the appearance of two new low-spin ferric heme signals at g=2.99 and at g=3.23 which are tentatively assigned to low-spin forms of cyanide-liganded cytochromed. With computer signal-averaging of the EPR spectrum of oxidized particles, the presence of resonances in the g=3–4 region could be demonstrated. These resonances are assigned to cytochromeb 1 (g-values at 3.68, 3.43),c-type cytochromes (g-values at 3.43, 3.25) and cytochromea 1, and possibly a low-spin form of ac-type cytochrome (g-value at 3.03). These EPR results represent, to our knowledge, the only such studies reported on the membrane-boundb 1 andc-type cytochromes of a bacterial respiratory-linked phosphorylating electron-transport chain.
    Type of Medium: Electronic Resource
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