Cys92, Cys101, Cys197, and Cys203 Are Crucial Residues for Coordinating the Iron–Sulfur Cluster of RhdA from Acidithiobacillus ferrooxidans |
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Authors: | Yunjie Dai Jianshe Liu Chunli Zheng Anna Wu Jia Zeng Guanzhou Qiu |
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Affiliation: | (1) Department of Bioengineering, School of Resources Processing and Bioengineering, Central South University, 410083 Changsha, Hunan, People’s Republic of China;(2) Department of Environmental Science & Engineering, Donghua University, 201620 Shanghai, People’s Republic of China |
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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. |
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