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  • 1
    Electronic Resource
    Electronic Resource
    Identification of cytochrome c oxidase in the alkaliphilic, obligately chemolithoautotrophic, sulfur-oxidizing bacterium ‘Thioalcalomicrobium aerophilum’ strain AL 3 (1999)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 179 (1999), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Cytochrome c oxidase from the novel alkaliphilic autotrophic sulfur bacterium ‘Thioalcalomicrobium aerophilum’ strain AL 3 was isolated and purified 87-fold. Spectroscopic analysis revealed the presence of both c- and b-type hemes as well as copper in a ratio of 3:2:1. The purified enzyme consists of three subunits with apparent molecular masses of 41, 34 and 32 kDa. The two small subunits contain covalently bound heme c. With TMPD as a substrate the pH optimum was determined to be pH 8.0. In the presence of monovalent cations the specific activity of the purified oxidase increased significantly. The enzyme was not able to oxidize external cytochrome c, but accepted electron from its native electron donor. The latter was separated from the other membrane cytochromes during anion-exchange chromatography and was identified as a high potential cytochrome c551. Overall the data indicate that the cytochrome c oxidase from this alkaliphilic autotrophic bacterium belongs to the heme-copper oxidase superfamily; regarding its subunit composition and content of prosthetic groups, the enzyme is similar in many aspects to the cbb3-type cytochrome c oxidases described for several neutrophilic bacteria, including anaerobic phototrophic and aerobic sulfur-oxidizing bacteria.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1999.tb08713.x
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  • 2
    Electronic Resource
    Electronic Resource
    A new soluble 10 kDa monoheme cytochrome c-552 from the anammox bacterium Candidatus“Kuenenia stuttgartiensis” (2005)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 252 (2005), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The chemolithoautotrophic anammox bacterium Candidatus“Kuenenia stuttgartiensis” grows anaerobically using ammonium as electron donor for nitrite reduction. More than 10% of the proteins in cell extracts of “K. stuttgartiensis” consist of c-type heme proteins. A 10 kDa soluble cytochrome c was purified from cell extracts using ultracentrifugation and anion exchange chromatography. The UV/Vis spectrum of the reduced cytochrome showed the γ, β and α absorption maxima at 419, 522 and 552 nm, respectively. The N-terminal amino acid sequence and peptide fragments of the tryptic digest of the protein were used to identify the corresponding gene. Analysis of the gene product showed that the protein was preceded by a 30 amino acids long leader sequence and that it belonged to the low-spin class ID cytochrome c. The CXXCH motive was located at the N-terminal site of the protein. The gene organization of the cytochrome showed some resemblance to cytochrome c clusters of unknown function in the genome of Nitrosomonas europaea and Geobacter sulfurreducens PCA.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/j.femsle.2005.09.007
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