Extracellular iron reductase activity produced by Listeria monocytogenes

Abstract

Little is known about how pathogenic microorganisms that do not produce low-molecular-weight iron-chelating agents, termed siderophores, acquire iron from their environment. We have identified an extracellular enzyme produced by Listeria monocytogenes that can mobilize iron from a variety of iron-chelate complexes via reduction of the metal. The iron reductase requires Mg²⁺, flavin mononucleotide (FMN), and reduced nicotinamide adenine dinucleotide (NADH) for activity. Saturation kinetics were found when initial velocity studies of iron reduction were carried out as a function of variable FMN concentrations in the presence of 100 μM NADH and 10 mM Mg²⁺. Hyperbolic kinetics were also found when these studies were repeated as a function of variable NADH concentrations along with 20 μM FMN and 10 mM Mg²⁺. This process of extracellular reduction, in all likelihood, could be involved in the mobilization of iron from soils and aqueous environments and from host tissues in pathogenic processes. This is the first report of the extracellular enzymic reduction of iron by microorganisms.