Relevance of ferritin-binding sites on isolated mitochondria to the mobilization of iron from ferritin.
Iron can be released from ferritin and utilized by isolated rat liver mitochondria for the synthesis of heme. Mobilization of iron from ferritin is initiated by the binding of ferritin to the mitochondria in an manner compatible with binding sites or receptors for ferritin on the mitochondria. The binding completes rapidly, it is independent of temperature, saturable, reversible and enhanced by K+ and Mg2+. The amount of ferritin binding sites is approx. 0.8 pmol/mg mitochondrial protein, and the affinity constant is 6.4 . 10(6)M-1. The binding kinetics correlate well with the functional features of the ferritin-mitochondrial interaction: i.e. mobilization of iron from ferritin followed by insertion of the iron into heme. The results support the concept of ferritin as a possible donor of iron to the mitochondria.
D000818:Animals; D005293:Ferritins / Q000378:metabolism*; D006736:Horses; D007501:Iron / Q000378:metabolism*; D033862:Iron-Binding Proteins; D007700:Kinetics; D008274:Magnesium / Q000494:pharmacology; D008930:Mitochondria, Liver / Q000187:drug effects / Q000378:metabolism*; D011188:Potassium / Q000494:pharmacology; D051381:Rats; D011956:Receptors, Cell Surface / Q000187:drug effects / Q000378:metabolism*; D013154:Spleen
D033862:Iron-Binding Proteins; D011956:Receptors, Cell Surface; C027293:ferritin receptor; D005293:Ferritins; D007501:Iron; D008274:Magnesium; D011188:Potassium