Beijing Nuclear Magnetic Resonance Center, College of Chemistry and Molecular Engineering, School of Life Sciences, Peking University, Beijing, 100871, China.
Protein Cell. 2012 Sep;3(9):714-21. doi: 10.1007/s13238-012-2051-4. Epub 2012 Aug 12.
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.
硫氧还蛋白(Grx)是一种同型二聚体,它通过两个谷胱甘肽(GSH)配体桥接[2Fe-2S]簇。在这项研究中,无论是单硫醇还是双硫醇的同型二聚体硫氧还蛋白都能够通过直接相互作用将其铁-硫(FeS)簇转移到脱辅基铁氧还蛋白(Fdx)上,而与同型二聚体硫氧还蛋白中 FeS 簇的稳定性无关。同型二聚体硫氧还蛋白中的配体 GSH 分子不稳定,可与游离 GSH 交换,从而抑制 FeS 簇从同型二聚体硫氧还蛋白向脱辅基铁氧还蛋白的转移。这一现象提示了 GSH 在 FeS 簇运输中的一个新作用。