Ferric iron is transported into Escherichia coli by a number of chelating compounds. Iron transport through the outer membrane by citrate, ferrichrome, enterobactin, aerobactin, yersiniabactin, and heme is catalyzed by highly specific proteins and across the cytoplasmic membrane by ABC transport systems with lower specificity. Transport across the outer membrane requires energy, which is provided by the proton motive force of the cytoplasmic membrane and transmitted to the outer membrane via the TonB-ExbB-ExbD proteins. Binding of substrates induces large long-range structural changes in the transport proteins, but does not open the channel. It is thought that the channel is opened by energy input from the cytoplasmic membrane. Although a basic understanding of how the transport proteins might function has been obtained from the crystal structures of three outer membrane proteins of E. coli and from many genetic and biochemical experiments, numerous fundamental questions still remain open. Transcription of the transport protein genes is regulated by the Fur protein, which when loaded with ferrous iron functions as a repressor. Fur also positively regulates genes of iron-containing proteins by repressing synthesis of an anti-sense RNA. Regulation of ferric citrate transport genes via a transmembrane device has become the paradigm of the regulation of a variety of systems, including the hypersensitivity response of plants to bacterial infections.