title: How does iron-sulfur cluster coordination regulate the activity of human glutaredoxin 2?
abstract: Human mitochondrial glutaredoxin (Grx2) was described as the first iron-sulfur protein from the thioredoxin superfamily of proteins. The [2Fe-2S] cluster was proposed to serve as redox sensor for the activation of Grx2 during oxidative stress. The authors have demonstrated that the iron-sulfur cluster is complexed by the two N-terminal active site thiols of two Grx2 monomers and two molecules of glutathione that are bound noncovalently to the proteins and in equilibrium with glutathione in solution. When reduced glutathione becomes the limiting factor for cluster coordination, the holo-Grx2 complex dissociates, yielding enzymatically active Grx2.
authors.affiliation: The Medical Nobel Institute for Biochemistry, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.
authors.forename: Carsten
authors.initials: C
authors.lastname: Berndt
authors.forename: Christoph
authors.initials: C
authors.lastname: Hudemann
authors.forename: Eva-Maria
authors.initials: EM
authors.lastname: Hanschmann
authors.forename: Rebecca
authors.initials: R
authors.lastname: Axelsson
authors.forename: Arne
authors.initials: A
authors.lastname: Holmgren
authors.forename: Christopher Horst
authors.initials: CH
authors.lastname: Lillig
mesh_terms: D005786:Gene Expression Regulation; D054477:Glutaredoxins; D005978:Glutathione / Q000378:metabolism; D006801:Humans; D007506:Iron-Sulfur Proteins / Q000235:genetics / Q000378:metabolism; D008928:Mitochondria / Q000378:metabolism; D008954:Models, Biological; D016297:Mutagenesis, Site-Directed; D010088:Oxidoreductases / Q000235:genetics / Q000378:metabolism*
chemical_list: C516008:GLRX2 protein, human; D054477:Glutaredoxins; D007506:Iron-Sulfur Proteins; D010088:Oxidoreductases; D005978:Glutathione