Glutathione regulates the transfer of iron-sulfur cluster from monothiol and dithiol glutaredoxins to apo ferredoxin.
10.1007/s13238-012-2051-4
- Author:
Lei WANG
1
;
Bingjie OUYANG
;
Yifei LI
;
Yingang FENG
;
Jean-Pierre JACQUOT
;
Nicolas ROUHIER
;
Bin XIA
Author Information
1. Beijing Nuclear Magnetic Resonance Center, College of Chemistry and Molecular Engineering, School of Life Sciences, Peking University, Beijing, 100871, China.
- Publication Type:Journal Article
- MeSH:
Circular Dichroism;
Dimerization;
Ferredoxins;
chemistry;
metabolism;
Glutaredoxins;
chemistry;
metabolism;
Glutathione;
metabolism;
Iron;
chemistry;
Ligands;
Magnetic Resonance Spectroscopy;
Sulfhydryl Compounds;
chemistry;
Sulfur;
chemistry;
Toluene;
analogs & derivatives;
chemistry
- From:
Protein & Cell
2012;3(9):714-721
- CountryChina
- Language:English
-
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.
