Glutathione regulates the transfer of iron-sulfur cluster from monothiol and dithiol glutaredoxins to apo ferredoxin
- 影响因子：
0.0
- DOI码：
10.1007/s13238-012-2051-4
- 发表刊物：
Protein Cell
- 摘要：
Holo glutaredoxin (Grx) is a homo-dimer that bridges a [2Fe-2S] cluster with two glutathione (GSH) ligands. In this study, both monothiol and dithiol holo Grxs are found capable of transferring their iron-sulfur (FeS) cluster to an apo ferredoxin (Fdx) through direct interaction, regardless of FeS cluster stability in holo Grxs. The ligand GSH molecules in holo Grxs are unstable and can be exchanged with free GSH, which inhibits the FeS cluster transfer from holo Grxs to apo Fdx. This phenomenon suggests a novel role of GSH in FeS cluster trafficking.
- 论文编号：
37
- 卷号：
3
- 页面范围：
714-21
- 是否译文：
否
- 发表时间：
2012-01-01
- 发布期刊链接：
- 第一作者：
Wang L
- 通讯作者：
Xia Bin
- 全部作者：
Rouhier N,Jacquot JP,Feng Y,Li Y,Ouyang B
