Frataxin Acts as an Iron Chaperone Protein to Modulate Mitochondrial Aconitase Activity.
Bulteau A-L, O’Neill HA, Kennedy MC, Ikeda-Saito M, Isaya G, Szweda LI
Science (2004)
Category: iron, mitochondria-biogenesis ¤ Added: Jul 12, 2004 ¤ Rating: ◊◊
Numerous degenerative disorders are associated with elevated levels of prooxidants and declines in mitochondrial aconitase activity. Deficiency in the mitochondrial iron-binding protein frataxin results in diminished activity of various mitochondrial iron-sulfur proteins including aconitase. We found that aconitase can undergo reversible citrate-dependent modulation in activity in response to pro-oxidants. Frataxin interacted with aconitase in a citrate-dependent fashion, reduced the level of oxidant-induced inactivation, and converted inactive [3Fe-4S]1+ enzyme to the active [4Fe-4S]2+ form of the protein. Thus, frataxin is an iron chaperone protein that protects the aconitase [4Fe-4S]2+ cluster from disassembly and promotes enzyme reactivation.