Functional, structural, and spectroscopic characterization of a glutathione-ligated [2Fe–2S] cluster in poplar glutaredoxin C1
作者： Nicolas Rouhier , Hideaki Unno , Sibali Bandyopadhyay , Lluis Masip , Sung-Kun Kim
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摘要: When expressed in Escherichia coli, cytosolic poplar glutaredoxin C1 (CGYC active site) exists as a dimeric iron-sulfur-containing holoprotein or monomeric apoprotein solution. Analytical and spectroscopic studies of wild-type protein site-directed variants structural characterization the by using x-ray crystallography indicate that contains subunit-bridging [2Fe-2S] cluster is ligated catalytic cysteines two glutaredoxins glutathiones. Mutagenesis data on variety suggest incorporation an iron-sulfur could be general feature plant possessing glycine adjacent to cysteine. In light these results, possible involvement oxidative stress sensing biosynthesis discussed with respect their intracellular localization.
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