Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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Assembly Mechanism of [$Fe_2S_2$] Cluster in Ferredoxin from Acidithiobacillus ferrooxidans

  • Chen, Qian (Department of Bioengineering, School of Resources Processing and Bioengineering, Central South University) ;
  • Mo, Hongyu (Department of Bioengineering, School of Resources Processing and Bioengineering, Central South University) ;
  • Tang, Lin (Center for Biomedical Engineering, Hunan University) ;
  • Du, Juan (Center for Biomedical Engineering, Hunan University) ;
  • Qin, Fang (Center for Biomedical Engineering, Hunan University) ;
  • Zeng, Jia (Department of Bioengineering, School of Resources Processing and Bioengineering, Central South University)
  • Received : 2010.05.13
  • Accepted : 2010.11.02
  • Published : 2011.02.28
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Abstract

Ferredoxin is a typical iron-sulfur protein that is ubiquitous in biological redox systems. This study investigates the in vitro assembly of a [$Fe_2S_2$] cluster in the ferredoxin from Acidithiobacillus ferrooxidans in the presence of three scaffold proteins: IscA, IscS, and IscU. The spectra and MALDI-TOF MS results for the reconstituted ferredoxin confirm that the iron-sulfur cluster was correctly assembled in the protein. The inactivation of cysteine desulfurase by L-allylglycine completely blocked any [$Fe_2S_2$] cluster assembly in the ferredoxin in E. coli, confirming that cysteine desulfurase is an essential component for iron-sulfur cluster assembly. The present results also provide strong evidence that [$Fe_2S_2$] cluster assembly in ferredoxin follows the AUS pathway.

Keywords

References

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