Current Microbiology

, 59:559

Cys92, Cys101, Cys197, and Cys203 Are Crucial Residues for Coordinating the Iron–Sulfur Cluster of RhdA from Acidithiobacillus ferrooxidans

Authors

  • Yunjie Dai
    • Department of Bioengineering, School of Resources Processing and BioengineeringCentral South University
    • Department of Environmental Science & EngineeringDonghua University
  • Chunli Zheng
    • Department of Bioengineering, School of Resources Processing and BioengineeringCentral South University
  • Anna Wu
    • Department of Bioengineering, School of Resources Processing and BioengineeringCentral South University
  • Jia Zeng
    • Department of Bioengineering, School of Resources Processing and BioengineeringCentral South University
  • Guanzhou Qiu
    • Department of Bioengineering, School of Resources Processing and BioengineeringCentral South University
Article

DOI: 10.1007/s00284-009-9476-x

Cite this article as:
Dai, Y., Liu, J., Zheng, C. et al. Curr Microbiol (2009) 59: 559. doi:10.1007/s00284-009-9476-x
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Abstract

By proteomic analysis, we found a rhodanese-like protein(RhdA) from Acidithiobacillus ferrooxidans ATCC 23270 whose C-terminal contained a cysteine motif (Cys-XX-Trp-XX-Cys), known to bind iron–sulfur clusters. But so far, there were no articles to confirm the existence of iron–sulfur cluster in RhdA. In this study, RhdA gene from A. ferrooxidans ATCC 23270 was cloned and expressed in Escherichia coli, the protein was purified by one-step affinity chromatography to homogeneity. The UV–Vis scanning and EPR spectra results indicated that the wild-type proteins contained an iron–sulfur cluster. Site-directed mutagenesis results revealed that the four cysteines Cys92, Cys101, Cys197, and Cys203 were crucial residues for iron–sulfur cluster binding.

Copyright information

© Springer Science+Business Media, LLC 2009