Frataxin acts as an iron chaperone protein to modulate mitochondrial aconitase activity

Anne Laure Bulteau, Heather A. O'Neill, Mary Claire Kennedy, Masao Ikeda-Saito, Grazia Isaya, Luke I. Szweda

Research output: Contribution to journalArticle

297 Scopus citations

Abstract

Numerous degenerative disorders are associated with elevated levels of pro-oxidants and declines in mitochondriat aconitase activity. Deficiency in the mitochondrial iron-binding protein frataxin results in diminished activity of various mitochondriat iron-sutfur 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.

Original languageEnglish (US)
Pages (from-to)242-245
Number of pages4
JournalScience
Volume305
Issue number5681
DOIs
StatePublished - Jul 9 2004

ASJC Scopus subject areas

  • General

Fingerprint Dive into the research topics of 'Frataxin acts as an iron chaperone protein to modulate mitochondrial aconitase activity'. Together they form a unique fingerprint.

  • Cite this

    Bulteau, A. L., O'Neill, H. A., Kennedy, M. C., Ikeda-Saito, M., Isaya, G., & Szweda, L. I. (2004). Frataxin acts as an iron chaperone protein to modulate mitochondrial aconitase activity. Science, 305(5681), 242-245. https://doi.org/10.1126/science.1098991