The ability of the siderophores aerobactin and enterochelin to remove iron from transferrin is reported. Aerobactin removes iron from both high-affinity sites on the transferrin molecule, but shows a marked preference for the C-terminal site. This preference is different to that of many iron chelators. Enterochelin removes iron perferentially from the N-terminal site. No evidence for synergism between aerobactin and bidentate ligands could be detected.
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