How does iron-sulfur cluster coordination regulate the activity of human glutaredoxin 2?

被引：85

作者：

Berndt, Carsten ^{[1
]}

Hudemann, Christoph ^{[1
]}

Hanschmann, Eva-Maria ^{[1
]}

Axelsson, Rebecca ^{[1
]}

Holmgren, Arne ^{[1
]}

Lillig, Christopher Horst ^{[1
]}

机构：

[1] Karolinska Inst, Dept Med Biochem & Biophys, Med Nobel Inst Biochem, SE-17177 Stockholm, Sweden

来源：

ANTIOXIDANTS & REDOX SIGNALING | 2007年 / 9卷 / 01期

关键词：

D O I：

10.1089/ars.2007.9.151

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

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页码：151 / 157

页数：7

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