Structural Basis for Delivery of the Intact [Fe2S2] Cluster by Monothiol Glutaredoxin

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• 作者：Thomas Iwema ; Antoine Picciocchi ; Daouda A. K. Traore ; Jean-Luc Ferrer ; Franck Chauvat ; Lilian Jacquamet
• 刊名：Biochemistry
• 出版年：2009
• 出版时间：July 7, 2009
• 年：2009
• 卷：48
• 期：26
• 页码：6041-6043
• 全文大小：737K
• 年卷期：v.48,no.26(July 7, 2009)
• ISSN：1520-4995

文摘

Glutaredoxins (GRX) are redox proteins which use glutathione as a cofactor and are divided into two classes, monothiol and dithiol. In each class, several GRX have been shown to form [Fe2S2] cluster coordinating homodimers. The dithiol GRX homodimer is proposed to serve as a sequestration form and its iron−sulfur cluster as an oxidative stress sensor. In contrast, the monothiol GRX homodimer has been suggested to act as a scaffold for [Fe2S2] cluster delivery. We present here the structure of a monothiol GRX homodimer (Escherichia coli GRX4) coordinating a [Fe2S2] cluster that reveals the structural basis of intact iron−sulfur cluster delivery.