This paper reviews and reports the results of experiments on the mechanism by which iron is delivered from extracellular transferrin to reticulocyte mitochondria in which haem is synthesized. It is suggested that transferrin donates the iron directly to mitochondria. Transferrin seems to be bound to mitochondria during the process of iron release. When the release of iron from transferrin is blocked by haem, the iron-transferrin complex remains bound to mitochondria so that the total amount of transferrin molecules associated with mitochondria increases in haem-treated reticulocytes. This also leads to an increase in the number of transferrin molecules in the cytosol. In haem-deficient reticulocytes, the rate of dissociation of iron from transferrin is accelerated and the uptake of iron by mitochondria is increased. When the synthesis of haem is inhibited, the non-haem iron in the cytosol (i.e. mainly low-molecular-weight and ferritin iron) comes from mitochondria. Greater amounts of non-haem iron can also be induced in reticulocytes incubated with highly saturated transferrin but, in this case, iron does not seem to be accumulated in mitochondria. These results represent an experimental basis for the elucidation of the excessive non-haem iron accumulation in erythroid cells observed in various clinical conditions.