Extracellular Iron Reductases: Identification of a New Class of Enzymes by Siderophore-Producing Microorganisms

This study identifies extracellular iron reductases in culture supernatant fluids of the siderophore-producing microorganismsEscherichia coliandPseudomonas aeruginosa.These enzymes were constitutively produced and reduced and released iron from a variety of ferric chelators. Dialyzable cofactors, necessary for the transfer of electrons in the enzymatic reduction of iron, were identified. The reductases were sensitive to treatment with proteinase K and guanidine–HCl, were not associated with siderophore activity, and were apparently released from the cell as extracellular enzymes. The acquisition of59Fe2+by cell suspensions ofE. coliandP. aeruginosawas saturable, suggesting that the ferrous iron generated by these reductases can be bound and transported.Salmonella typhimuriummutantsfeoB, tonB, entB,andentBfeoB,deficient in numerous known iron uptake pathways, were found to exhibit substantial extracellular iron-reducing activities over that of the parent. A hypothesis is proposed in which the extracellular iron reductases excreted by siderophore-producing microorganisms may be responsible for the mobilization of iron during conditions of iron repletion when siderophores are repressed and may also function in concert with siderophores during periods of iron starvation.