Frataxin acts as an iron chaperone protein to modulate mitochondrial aconitase activity.
Bulteau, AL O'Neill, HA Kennedy, MC Ikeda-Saito, M Isaya, G Szweda, LI
||Bulteau AL, etal., Science 2004 Jul 9;305(5681):242-5.
||(View Article at PubMed) PMID:15247478
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.
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