scholarly journals Spectroscopic characterization of the novel iron-sulfur cluster in Pyrococcus furiosus ferredoxin.

1990 ◽  
Vol 265 (15) ◽  
pp. 8533-8541
Author(s):  
R C Conover ◽  
A T Kowal ◽  
W G Fu ◽  
J B Park ◽  
S Aono ◽  
...  
1997 ◽  
Vol 36 (2) ◽  
pp. 214-219 ◽  
Author(s):  
Yuheng Deng ◽  
Qiutian Liu ◽  
Yu Yang ◽  
Youtong Wang ◽  
Yuanba Cai ◽  
...  

1981 ◽  
Vol 20 (11) ◽  
pp. 3586-3589 ◽  
Author(s):  
Pierre. Braunstein ◽  
Antonio. Tiripicchio ◽  
Marisa. Tiripicchio Camellini ◽  
Enrico. Sappa

2007 ◽  
Vol 104 (18) ◽  
pp. 7379-7384 ◽  
Author(s):  
Nicolas Rouhier ◽  
Hideaki Unno ◽  
Sibali Bandyopadhyay ◽  
Lluis Masip ◽  
Sung-Kun Kim ◽  
...  

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.


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