Galline Ex-FABP was identified as another candidate antibacterial, catecholate siderophore
binding lipocalin (siderocalin) based on structural parallels with the family archetype …

Siderophores, denned as high affinity iron (III) ion transport agents, and their cognate
membrane‐bound receptor complexes, occur in the enteric bacteria Escherichia coli and …

Marinobactins A–E are a suite of amphiphilic siderophores which have a common peptidic
head group that coordinates Fe (III), and a fatty acid which varies in length and saturation. As …

Synthetic enterobactin and enantioenterobactin (D-seryl enterobactin) have been examined
for the ability to transport iron in Escherichia coli. Failure of the unnatural, D-serine-derived …

Synthetic analogs of enterochelin (enterobactin) were tested for their ability to support the
growth of Escherichia coli K-12 under iron-limiting conditions. The cyclic compound MECAM …

Enterobactin (ENT) is a tris-catechol siderophore used to acquire iron by multiple bacterial
species. These ENT-dependent iron uptake systems have often been considered as …

Salmonella typhimurium possesses two outer membrane receptor proteins, IroN and FepA,
which have been implicated in the uptake of enterobactin. To determine whether both …

In Escherichia coli, the outer membrane protein FepA is a receptor for the siderophore
complex ferric enterobactin and for colicins B and D. To identify protein domains important …

Bacteria secrete small molecules known as siderophores to acquire iron from their
surroundings. For over 60 years, investigations into the bioinorganic chemistry of these …

Most high-affinity systems for iron uptake in Gram-negative bacteria are thought to employ
periplasmic-binding-protein-dependent transport. In Escherichia coli, FepB is a periplasmic …