期刊
PROTEIN & CELL
卷 3, 期 9, 页码 714-721出版社
OXFORD UNIV PRESS
DOI: 10.1007/s13238-012-2051-4
关键词
iron-sulfur cluster; glutaredoxin; glutathione; ferredoxin; CD; NMR
类别
资金
- Ministry of Science and Technology of China [2012CB910703, 2006DFA31210]
- National Natural Science Foundation of China [30570353]
- ANR [2010BLAN1616]
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.
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