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  • Blackwell Publishing Ltd  (2)
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  • 1
    Electronic Resource
    Electronic Resource
    Isolation, characterization and crystallization of an iron-superoxide dismutase from the crenarchaeon Sulfolobus acidocaldarius (1996)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 138 (1996), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract An iron containing Superoxide dismutase from the cytosol of the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius (DSM 639) has been purified to electrophoretic homogeneity. It comprises at least 11% of the cytosolic protein. The isolated protein consists of two identical subunits with an apparent molecular mass of 22.4 kDa. It contains one iron atom per dimer. The protein shows the typical EPR spectrum of a S = 3 / 2, rhombic high-spin iron center. It is extremely resistant against thermal and chemical denaturation. Simultaneous treatment with heat and detergent resulted in the conversion into a more active tetrameric form. Similar enzymes appear to be present in the cytosol of other members of the Sulfolobaceae. The dimeric form of the protein from S. acidocaldarius has been crystallized.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1996.tb08136.x
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  • 2
    Electronic Resource
    Electronic Resource
    A cytochrome aa3-type quinol oxidase from Desulfurolobus ambivalens, the most acidophilic archaeon (1994)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 117 (1994), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Membranes of the extremely thermoacidophilic archaeon Desulfurolobus ambivalens grown under aerobic conditions contain a quinol oxidase of the cytochrome aa3-type as the most prominent hemoprotein. The partially purified enzyme consists of three polypeptide subunits with apparent molecular masses of 40, 27 and 20 kDa and contains two heme A molecules and one copper atom. CO difference spectra suggest one heme to be a heme a3-centre. The EPR spectra indicate the presence of a low-spin and a high-spin heme species. Redox titrations of the solubilized enzyme show the presence of two reduction processes, with apparent potentials of + 235 and + 330 mV. The enzyme cannot oxidize reduced cytochrome c, but rather serves as an oxidase of caldariella quinone. Due to their very simple composition, D. ambivalens cell appear as a promising candidate to study Structure-function relationships of cytochrome aa3 in the integral membrane state.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1994.tb06779.x
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