| Literature DB >> 17909890 |
Jia Zeng1, Xia Huang, Yuandong Liu, Jianshe Liu, Guanzhou Qiu.
Abstract
The [2Fe-2S] cluster containing ferredoxin has attracted much attention in recent years. Genetic analyses show that it has an essential role in the maturation of various iron-sulfur (Fe-S) proteins and functions as a component of the complex machinery responsible for the biogenesis of Fe-S clusters. The gene of ferredoxin from A. ferrooxidans ATCC 23270 was cloned, successfully expressed in Escherichia coli, and purified by one-step affinity chromatography to homogeneity. The MALDI-TOF MS and spectra results of the recombinant protein confirmed that the iron-sulfur cluster was correctly inserted into the active site of the protein. Site-directed mutagenesis results revealed that Cys42, Cys48, Cys51, and Cys87 were ligating with the [Fe(2)S(2)] cluster of the protein.Entities:
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Year: 2007 PMID: 17909890 DOI: 10.1007/s00284-007-9025-4
Source DB: PubMed Journal: Curr Microbiol ISSN: 0343-8651 Impact factor: 2.188