Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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Functional Roles of the Aromatic Residues in the Stabilization of the [$Fe_4S_4$] Cluster in the Iro Protein from Acidithiobacillus ferrooxidans

  • Zeng, Jia (Center for Biomedical Engineering, State Key Laboratory of Chemo/Biosensing and Chemometrics, Hunan University) ;
  • Liu, Qing (Department of Bioengineering, Central South University) ;
  • Zhang, Xiaojian (Department of Bioengineering, Central South University) ;
  • Mo, Hongyu (Department of Bioengineering, Central South University) ;
  • Wang, Yiping (Department of Bioengineering, Central South University) ;
  • Chen, Qian (Department of Bioengineering, Central South University) ;
  • Liu, Yuandong (Department of Bioengineering, Central South University)
  • Published : 2010.02.28
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Abstract

The Iro protein is a member of the HiPIP family with the [$Fe_4S_4$] cluster for electron transfer. Many reports proposed that the conserved aromatic residues might be responsible for the stability of the iron-sulfur cluster in HiPIP. In this study, Tyr10 was found to be a critical residue for the stability of the [$Fe_4S_4$] cluster, according to site-directed mutagenesis results. Tyr10, Phe26, and Phe48 were essential for the stability of the [$Fe_4S_4$] cluster under acidic condition. Trp44 was not involved in the stability of the [$Fe_4S_4$] cluster. Molecular structure modeling for the mutant Tyr10 proteins revealed that the aromatic group of Tyr10 may form a hydrophobic barrier to protect the [$Fe_4S_4$] cluster from solvent.

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References

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