Glutathione-dependent oxidoreductase that facilitates the maintenance of mitochondrial redox homeostasis upon induction of apoptosis by oxidative stress. Involved in response to hydrogen peroxide and regulation of apoptosis caused by oxidative stress. Acts as a very efficient catalyst of monothiol reactions because of its high affinity for protein glutathione-mixed disulfides. Can receive electrons not only from glutathione (GSH), but also from thioredoxin reductase supporting both monothiol and dithiol reactions. Efficiently catalyzes both glutathionylation and deglutathionylation of mitochondrial complex I, which in turn regulates the superoxide production by the complex. Overexpression decreases the susceptibility to apoptosis and prevents loss of cardiolipin and cytochrome c release.
[1]"Reversible sequestration of active site cysteines in a 2Fe-2S-bridged dimer provides a mechanism for glutaredoxin 2 regulation in human mitochondria."Johansson C., Kavanagh K.L., Gileadi O., Oppermann U.J. Biol. Chem. 282:3077-3082(2007). [2]"Solution structure of RSGI RUH-044, an N-terminal 2 domain of glutaredoxin 2 from human cDNA." RIKEN structural genomics initiative (RSGI)Submitted (NOV-2005). [3]"Characterization of human glutaredoxin 2 as iron-sulfur protein: a possible role as redox sensor." Lillig C.H., Berndt C., Vergnolle O., Loenn M.E., Hudemann C., Bill E., Holmgren A.Proc. Natl. Acad. Sci. U.S.A. 102:8168-8173(2005).
