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Isolation Of A Siderophore Produced By Methicillin-Resistant Staphylococcus Aureus Strain H372., Rachel Elizabeth Presswood
Isolation Of A Siderophore Produced By Methicillin-Resistant Staphylococcus Aureus Strain H372., Rachel Elizabeth Presswood
Electronic Theses and Dissertations
Iron is necessary for many cellular processes such as the electron transport chain and gene regulation. However, most iron on earth is found in insoluble iron-hydroxide complexes. In addition, iron is tightly sequestered in the human body by proteins such as transferrin, making it unavailable for pathogens. In order to overcome these limitations bacteria have evolved siderophores. Siderophores are low molecular weight compounds that bind ferric iron with a high affinity. Staphylococcus aureus is an important human pathogen that is known to produce at least four siderophores, and these siderophores contribute to its virulence. S. aureus strain H372 was found …
Isolation And Identification Of The Siderophore "Vicibactin" Produced By Rhizobium Leguminosarum Atcc 14479., William H. Wright Iv
Isolation And Identification Of The Siderophore "Vicibactin" Produced By Rhizobium Leguminosarum Atcc 14479., William H. Wright Iv
Electronic Theses and Dissertations
Siderophores are small, iron chelating molecules produced by many bacteria to help meet the iron requirements of the cell. Multiple metabolic functions require iron as it serves as a cofactor in many enzymes and cellular processes. However, in the presence of oxygen and at physiologic pH, iron forms insoluble ferric complexes that cause the nutrient to be unavailable to bacterial cells. Siderophores alleviate this limitation by chelating the ferric iron, rendering it soluble and available for uptake. One group of microorganisms known for their ability to produce siderophores is the rhizobia. These bacteria are characterized both by their formation of …
Molecular Mechanism Of Ferricsiderophore Transport Via The Outer Membrane Receptor Fhua In Escherichia Coli., Jennifer K. Cooke
Molecular Mechanism Of Ferricsiderophore Transport Via The Outer Membrane Receptor Fhua In Escherichia Coli., Jennifer K. Cooke
Electronic Theses and Dissertations
Iron is essential for life and growth in most organisms. Although it is abundant, iron exists mostly as insoluble iron-oxyhydroxide. Bacteria secrete siderophores to chelate iron and transport it into the cell via specific outer membrane receptors. The FhuA receptor protein transports ferrichrome, a siderophore produced by Ustilago sphaerogena. 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 role in ferrichrome transport. We hypothesize that during transport the plug domain of FhuA does not leave the barrel; rather it undergoes …
Iron Acquisition In Rhodococcus Erythropolis Strain Igts8: Characterization Of A Mutant Strain That Over Produces Siderophore., Melanie Anne Pratt
Iron Acquisition In Rhodococcus Erythropolis Strain Igts8: Characterization Of A Mutant Strain That Over Produces Siderophore., Melanie Anne Pratt
Electronic Theses and Dissertations
Iron is an essential nutrient for most bacteria because enzymes like nitrate reductase and cytochromes use it as a cofactor. However, in most aerobic, neutral pH environments, iron is essentially insoluble and not easily available for bacteria to use. Many bacteria respond to this problem by releasing small organic compounds called siderophores that bind and effectively solubilize iron so that it can be transported into the cell for growth. The focus of this study was to learn more about the iron acquisition and especially the transport of iron by the soil bacterium Rhodococcus erythropolis. To fulfill this aim, mutant …