Characterization of a novel ferredoxin with N-terminal extension from Clostridium acetobutylicum ATCC 824

被引:0
|
作者
Razia Kutty
George N. Bennett
机构
[1] Rice University,Department of Biochemistry and Cell Biology MS
来源
Archives of Microbiology | 2007年 / 187卷
关键词
Ferredoxin; Polyferredoxin; Electron acceptors; Trinitrotoluene biotransformation; Hydrogenase; Iron storage proteins; Iron–sulfur clusters;
D O I
暂无
中图分类号
学科分类号
摘要
A gene (CAC2657) encoding a ferredoxin (EFR1) from the strictly anaerobic soil bacterium Clostridium acetobutylicum was cloned and expressed in Escherichia coli. The ferredoxin gene encodes a polypeptide of 27 kDa that incorporates 2[4Fe–4S] clusters. An extended N-terminal region of 187 amino acid (aa) residues precedes ferredoxin domain. The EFR1 expressed in E. coli is a trimeric protein. The iron and sulfur content of the reconstituted protein agrees with that expected of a trimeric form of the protein. The ferredoxin domain of EFR1 is closely related to ferredoxin of C. pasteurianum; and can be fitted to the X-ray crystal structure with a root mean square deviation of 0.62 As for the Cα atoms of the generated 3D simulation model. In cultures of C. acetobutylicum the efr1 gene shows higher relative expression on induction with Trinitrotoluene (TNT) compared to that from uninduced control cultures.
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页码:161 / 169
页数:8
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