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Showing 1 to 4 of 4 for “"Ferrichrome"”.

  1. Molecular Mechanism of Ferricsiderophore Transport via the Outer Membrane Receptor FhuA in <em>Escherichia coli</em>.

    … receptors. The FhuA receptor protein transports ferrichrome, a siderophore produced by <em>Ustilago sphaerogena</em>. We determined the binding affinity of variants from the conserved 'lock region' of FhuA and also created and characterized variants of the highly conserved R452 to determine its …

    etsu Repository record for Molecular Mechanism of Ferricsiderophore Transport via the Outer Membrane Receptor FhuA in <em>Escherichia coli</em>. (opens in a new tab)

  2. Haem and xenosiderophore mediated iron acquisition by sinorhizobium meliloti and pseudomonas aeruginosa

    … FhuA1 and FhuA2 function in the utilisation of ferrichrome and ferrioxamine B respectively. Analysis of the region directly downstream of FhuA2 resulted in the identification of a ferrioxamine B specific ferric iron reductase, fhuF (smc01658), and a periplasmic siderophore binding protein, fhuP …

    dcu Repository record for Haem and xenosiderophore mediated iron acquisition by sinorhizobium meliloti and pseudomonas aeruginosa (opens in a new tab)

  3. Biochemical characterization of Aspergillus fumigatus SidA: a flavin-dependent N-hydroxylating enzyme

    Ferrichrome is a hydroxamate-containing siderophore produced by the pathogenic fungus Aspergillus fumigatus during infection. This siderophore includes N5-hydroxylated L-ornithine in the peptide backbone that serve as iron chelators. Af SidA is the L-ornithine N5-hydroxylase, which performs the …

    vt Repository record for Biochemical characterization of Aspergillus fumigatus SidA: a flavin-dependent N-hydroxylating enzyme (opens in a new tab)

  4. Characterization of FhuA 104/149C: a Double Cysteine FhuA Mutant with Normal Binding and Diminished Transport

    … severely reduced transport of radio-labeled ferrichrome. In the course of this study, this protein was HPLC purified for structural studies by crystallization and X-ray diffraction. In addition, protein interaction studies were performed with purified TonB-C terminal revealing no impact of …

    etsu Repository record for Characterization of FhuA 104/149C: a Double Cysteine FhuA Mutant with Normal Binding and Diminished Transport (opens in a new tab)