| Literature DB >> 22886498 |
Lei Wang1, Bingjie Ouyang, Yifei Li, Yingang Feng, Jean-Pierre Jacquot, Nicolas Rouhier, Bin Xia.
Abstract
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.Entities:
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Year: 2012 PMID: 22886498 PMCID: PMC4875373 DOI: 10.1007/s13238-012-2051-4
Source DB: PubMed Journal: Protein Cell ISSN: 1674-800X Impact factor: 14.870