| 20208432 |
Zeng J, Liu Q, Zhang X, Mo H, Wang Y, Chen Q, Liu Y: Functional roles of the aromatic residues in the stabilization of the [Fe4S4] cluster in the Iro protein from Acidithiobacillus ferrooxidans. J Microbiol Biotechnol. 2010 Feb;20(2):294-300.
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. |
1(0,0,0,1) |