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J. Microbiol. Biotechnol. 2010; 20(2): 294-300

Published online February 28, 2010 https://doi.org/10.4014/jmb.0906.06040

Copyright © The Korean Society for Microbiology and Biotechnology.

Functional roles of the aromatic residues in the stabilization of the [Fe4S4] cluster in the Iro protein from Acidithiobacillus ferrooxidans

Jia Zeng 1*, Qing Liu 2, Xiaojian Zhang 2, Hongyu Mo 2, Yiping Wang 2, Qian Chen 2 and Yuandong Liu 2

1Center for Biomedical Engineering, State Key Laboratory of Chemo/Biosensing and Chemometrics, Hunan University, ChangshaHunan 410082, P. R. China , 2Department of Bioengineering, Central South University, Changsha, Hunan 410083, P. R. China

Received: June 23, 2009; Accepted: August 31, 2009

Abstract

The Iro protein is a member of HiPIP family with the [Fe4S4] 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 [Fe4S4] cluster according to site-directed mutagenesis results. Tyr10, Phe26 and Phe48 were essential for the stability of the [Fe4S4] cluster under acidic condition. Trp44 were not involved in the stability of the [Fe4S4] cluster. Molecular structure modeling for the mutant Tyr10 proteins revealed that the aromatic group of Tyr10 may form a hydrophobic barrier to protect the [Fe4S4] cluster from solvent.

Keywords: Acidithiobacillus ferrooxidans, Iro protein, Iron-sulfur cluster, Mutation, Molecular modeling