A [2Fe-2S] protein from the hyperthermophilic bacterium Aquifex aeolicus

被引:22
作者
Chatelet, C
Gaillard, J
Pétillot, Y
Louwagie, M
Meyer, J
机构
[1] CEA Grenoble, Dept Biol Mol & Struct, F-38054 Grenoble, France
[2] CEA Grenoble, Dept Rech Mat Condensee SCIB, F-38054 Grenoble, France
[3] CNRS, CEA, Inst Biol Struct, F-38027 Grenoble, France
关键词
D O I
10.1006/bbrc.1999.1138
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Overexpression in Escherichia coli of the fdx4 gene from Aquifex aeolicus has allowed isolation and characterization of the first hyperthermophilic [2Fe-2S](Scys)(4) protein, a homodimer of M = 2 x 12.4 kDa with one [2Fe-2S] cluster per subunit, This protein is undamaged by heating to 100 degrees C for at least three hours. The primary structure, in particular the characteristic distribution of the four cysteine ligands of the metal site, and the spectroscopic properties of the A. aeolicus protein relate it to well characterized [2Fe-2S] proteins from Clostridium pasteurianum and Azotobacter vinelandii, These proteins are also homologous to subunits or domains of hydrogenases and NADH-ubiquinone oxidoreductase (Complex I) of respiratory chains. The A. aeolicus [2Fe-2S] protein is thus representative of a presumably novel protein fold involved in a variety of functions in very diverse cellular backgrounds. (C) 1999 Academic Press.
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页码:885 / 889
页数:5
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