Frataxin acts as an iron chaperone protein to modulate mitochondrial aconitase activity |
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| Authors: | Bulteau Anne-Laure O'Neill Heather A Kennedy Mary Claire Ikeda-Saito Masao Isaya Grazia Szweda Luke I |
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| Institution: | Department of Physiology and Biophysics, Case Western Reserve University, Cleveland, OH, USA. |
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| Abstract: | 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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