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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    BioMetals 9 (1996), S. 185-189 
    ISSN: 1572-8773
    Keywords: rhizoferrin ; metal complexes ; transport ; siderophores ; iron
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Rhizoferrin-mediated iron uptake was studied in two different classes of organisms: a rhizoferrin producing fungus, Absidia spinosa (Zygomycetes), and a ferric rhizoferrin utilizing bacterium, Morganella morganii (Enterobacteriaceae). The uptake of iron rhizoferrin and some of its metal analogs (chromium, rhodium, gallium), was followed and kinetic parameters measured in A. spinosa. These metal ion complexes were taken up in a concentration- and energy-dependent manner indicative of an active transport system. The uptake of the kinetically inert chromium and rhodium and reductively inert gallium complexes suggests a variation of the so called ‘shuttle’ mechanism may be operative. The recognition of one geometrical isomer of chromium-rhizoferrin but not another argues for a degree of stereospecificity in the uptake process. A growth promotion plate assay was used to examine metal-rhizoferrin uptake in M. morganii. The results indicate that a number of factors including the nature of the chelating agent (e.g. bipyridyl or EDDHA) used to induce iron deficiency need to be considered before these simple plate assays can be reliably used to indicate the presence or absence of a particular siderophore uptake system.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1572-8773
    Keywords: Escherichia coli ; ferrioxamine receptor ; iron transport ; photoaffinity label ; siderophores
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The photoreactivep-azidobenzoyl analog of ferrioxamine B was used to show that ferrioxamine-B-mediated iron transport is separate and distinct from coprogen-mediated iron transport inEscherichia coli. Photolysis of this analog inhibited uptake of [59Fe]ferrioxamine B but not [59Fe]coprogen or [59Fe]ferrichrome. Conversely, photolysis of thep-azidobenzoyl analog of coprogen B inhibited uptake of [59Fe]coprogen but not [59Fe]ferrioxamine B or [59Fe]ferrichrome. Photolabeling of outer membranes withp-azidobenzoyl-[59Fe]ferrioxamine B resulted in the labeling of two iron-regulated peptides with molecular masses of about 66 and 26 kDa. Expression of these peptides was increased when ferrioxamine B was the sole iron source. Both peptides were present in outer membrane preparations of thefhuF mutant H1717, but the 66 kDa peptide was not inducible. These results are evidence for an outer membrane receptor inE. coli unique for linear ferrioxamines.
    Type of Medium: Electronic Resource
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