Inorganic iron can be transported into cells in the absence of transferrin. Ferric iron enters cells utilizing an integrin-mobilferrin pathway, whereas ferrous iron uptake is facilitated by divalent metal transporter-a (DMT-1). Immunoprecipitation studies using anti-mobilferrin antibody precipitated the previously described large molecular weight protein complex named paraferritin. It was previously shown that paraferritin functions as a ferrireductase reducing ferric iron to ferrous iron utilizing NADPH as the energy source. It functions in the pathway for the cellular uptake of ferric iron. This multi-peptide protein contains a number of active peptides including the ferric iron binding protein mobilferrin, and a flavin mono-oxygenase. The immunoprecipitates and purified preparations of paraferritin also contained DMT-1. This identifies DMT-1 as one of the peptides constituting the paraferritin complex. Since paraferritin functions to reduce newly transported ferric iron to ferrous iron, and DMT-1 can transport ferrous iron, these findings suggest a role for DMT-1 in conveyance of iron from paraferritin to ferrocheletase, the enzyme utilizing ferrous iron for the synthesis of heme in the mitochondrion.