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- Title
Expression, Purification, and Characterization of a [Fe<sub>2</sub>S<sub>2</sub>] Cluster Containing Ferredoxin from Acidithiobacillus ferrooxidans.
- Authors
Jia Zeng; 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 [Fe2S2] cluster of the protein.
- Subjects
FERREDOXIN-NADP reductase; SULFUR amino acids; MOLECULAR evolution; ESCHERICHIA coli; PROTEIN synthesis; CLUSTERING of particles; MUTAGENS; CLUSTER analysis (Statistics); PHYSICAL sciences research
- Publication
Current Microbiology, 2007, Vol 55, Issue 6, p518
- ISSN
0343-8651
- Publication type
Article
- DOI
10.1007/s00284-007-9025-4