GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.
Bulteau, AL, O'Neill, HA, Kennedy, MC, Ikeda-Saito, M, Isaya, G and Szweda, LI (2004) Frataxin acts as an iron chaperone protein to modulate mitochondrial aconitase activity. Science 305:242-5
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.
Aconitate Hydratase/antagonists & inhibitors; Aconitate Hydratase/metabolism; Animals; Citric Acid/metabolism; Citric Acid/pharmacology; Dithiothreitol/metabolism; Electron Spin Resonance Spectroscopy; Enzyme Activation; Ferrous Compounds/metabolism; Hydrogen Peroxide/pharmacology; Iron/metabolism; Iron-Binding Proteins/metabolism; Male; Mitochondria/metabolism; Mitochondria, Heart/metabolism; Molecular Chaperones/metabolism; Oxidation-Reduction; Oxidative Stress; Oxygen Consumption; Rats; Rats, Sprague-Dawley; Saccharomyces cerevisiae/metabolism; Saccharomyces cerevisiae Proteins/metabolism
|Gene product||Qualifier||GO ID||GO term name||Evidence Code||with/from||Aspect||Notes||Status|
See Help:References for how to manage references in GONUTS.