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  • 1
    Electronic Resource
    Electronic Resource
    The 44-kDa c-type cytochrome induced in Rhodobacter capsulatus during growth with dimethylsulphoxide as an electron acceptor is a cytochrome c peroxidase (1992)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 97 (1992), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract A 44-kDa c-type cytochrome was purified from membranes of Rhodobacter capsulatus. The cytochrome contained an ascorbate-reducible haem (α-max 556 nm) and a dithionite-reducible haem (α-max 552 nm) and had catalytic properties which indicated that it was a cytochrome c peroxidase. Increased levels of this cytochrome were observed when dimethylsulphoxide was present during phototrophic growth of cells but this was not observed when trimethylamine-N-oxide was present. The results indicate that the 44-kDa cytochrome is probably not directly involved in the dimethylsulphoxide/trimethylamine-N-oxide respiratory pathway of Rhodobacter capsulatus.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1992.tb05476.x
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    formation for phenylethylamine oxidase expressed in Escherichia coli K-12 (1995)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 133 (1995), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Arthrobacter globiformis amine oxidase produced by Escherichia coli cells grown in copper-depleted media was reported to undergo activation due to formation of its topaquinone cofactor in a copper-dependent autocatalytic reaction. Likewise, a mutated E. coli amine oxidase located in the cytoplasm was reported to form topaquinone autocatalytically in an EDTA-sensitive reaction. Here we show unequivocally that formation of an amine oxidase lacking topaquinone is primarily a consequence of the location of the enzyme in the cytoplasm rather than the level of copper in the growth medium. For E. coli, insertion of copper into apoamine oxidase and subsequent topaquinone formation occur after export of the apoenzyme into the periplasm.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1995.tb07896.x
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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