Enterobactin is a catechol-type siderophore primarily found in Gram-negative bacteria that transports and sequesters iron in bacteria. It has very extremely high affinity for ferric ions (K = 1052 10-1M). Ferric enterobactin complexes are recognised by outer-membrane transporters and imported into the periplasm in a process dependent on the inner-membrane protein TonB. In E. coli, enterobactin binds to the periplasmic protein, FepB. Enterobactin is a dimer of 2,3-dihydroxybenzoic acid.
- Enterobactin, an iron transport compound from Salmonella typhimurium.Pollack J.R. and Neilands J.B. Biochem Biophys Res Comm. 1970, 68, 2870.
- The structure of enterochelin and related 2,3-dihydroxy-N-benzoyne conjugates from Eschericha Coli. O'Brien I.G. and Gibson T. Biochim Biophys Acta 1970, 215, 393.
- Ferric ion sequestering agents. 2. Kinetics and mechanism of iron removal from transferrin by enterobactin and synthetic tricatechols. Carrano C.J. and Raymond K.N. J Am Chem Soc. 1979, 101, 5401.
- Binding of ferric enterobactin by the Escherichia coli periplasmic protein FepB. Sprencel C. et al. J Bacteriol. 2000, 182, 5359.