Journal
SCIENCE
Volume 305, Issue 5681, Pages 242-245Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1098991
Keywords
-
Categories
Funding
- NIA NIH HHS [AG-16339, AG-15709] Funding Source: Medline
- NINR NIH HHS [NRSA 44748] Funding Source: Medline
Ask authors/readers for more resources
Numerous degenerative disorders are associated with elevated levels of pro-oxidants 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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available