Functional, structural, and spectroscopic characterization of a glutathione-ligated [2Fe-2S] cluster in poplar glutaredoxin C1.

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

Citation

Nicolas Rouhier, Hideaki Unno, Sibali Bandyopadhyay, Lluis Masip, Sung-Kun Kim, Masakazu Hirasawa, José Manuel Gualberto, Virginie Lattard, Masami Kusunoki, David B Knaff, George Georgiou, Toshiharu Hase, Michael K Johnson, Jean-Pierre Jacquot. Functional, structural, and spectroscopic characterization of a glutathione-ligated [2Fe-2S] cluster in poplar glutaredoxin C1. Proceedings of the National Academy of Sciences of the United States of America. 2007 May 01;104(18):7379-84

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PMID: 17460036

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