Mitochondria have Fe(III) receptors.
Recent work has provided new evidence that ATP is the major constituent of the low-Mr iron pool in the reticulocyte. The interaction of the iron complex of ATP with mitochondria was investigated in the present experiments. When ATP-Fe3+ was incubated with mitochondria, Fe3+, free of ATP, bound with high affinity to Fe3+ receptors on the mitochondria. The binding was saturable and reversible. Iron which was complexed to PPi, nitrilotriacetate, citrate, ADP and GTP also showed saturable binding to mitochondria; Fe3+ complexed to AMP bound non-specifically, as did Fe2+/ascorbate complexed to AMP bound non-specifically, as did Fe2+/ascorbate and Fe2+/dithionite.
Weaver
J
J
Department of Medicine, Albert Einstein College of Medicine, Bronx, NY 10461.
Zhan
H
H
Pollack
S
S
D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D007501:Iron / Q000378:metabolism*; D007700:Kinetics; D008024:Ligands; D008930:Mitochondria, Liver / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains; D011956:Receptors, Cell Surface / Q000378:metabolism*
C062861:Fe(III) receptor, rat; D008024:Ligands; D011956:Receptors, Cell Surface; D000255:Adenosine Triphosphate; D007501:Iron