Active transport of iron and siderophore antibiotics |
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| Authors: | Braun Volkmar Braun Michael |
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| Institution: | 2. i3S - Instituto de Investigação e Inovação em Saúde, Universidade do Porto, Portugal;3. IBMC-Instituto de Biologia Molecular e Celular, 4150-180 Porto, Portugal;4. ICBAS- Instituto de Ciências Biomédicas Abel Salazar, Universidade do Porto, Portugal;1. Institute of Cosmetology, Public Higher Medical Professional School in Opole, Opole, Poland;2. Department of Organic Chemistry, The Weizmann Institute of Science, Rehovot, Israel;3. University of Michigan College of Pharmacy, Ann Arbor, MI, USA;4. University of Michigan Health System, Ann Arbor, MI, USA;5. Faculty of Chemistry, University of Wrocław, Wrocław, Poland |
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| Abstract: | Bacteria solubilize iron (Fe(3+)) with secreted siderophores, which are then taken up as Fe(3+)-siderophore complexes. Some bacteria also use iron in heme, hemoglobin, hemopexin, transferrin and lactoferrin of eukaryotic hosts. Crystal structures of two outer membrane transport proteins, FhuA and FepA, and biochemical data reveal strong long-range conformational changes of the proteins upon binding of Fe(3+)-siderophore complexes and in response to energy transfer from the cytoplasmic membrane into the outer membrane via the TonB-ExbB-ExbD protein complex. The crystal structure of the periplasmic binding protein FhuD strongly deviates from the uniform overall structure of binding proteins hitherto determined. Sideromycins, antibiotics that contain Fe(3+)-siderophore complexes as carriers, are highly effective, as they enter cells via Fe(3+)-siderophore transport systems. In this review, recently published data is discussed to demonstrate the state of understanding of iron transport across the outer membrane and the cytoplasmic membrane. |
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