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Expression, purification and characterization of a cysteine desulfurase, IscS, from Acidithiobacillus ferrooxidans

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Abstract

Iron–sulfur clusters are one of the most common types of redox center in nature. Three proteins of IscS (a cysteine desulfurase), IscU (a scaffold protein) and IscA (an iron chaperon) encoded by the operon iscSUA are involved in the iron–sulfur cluster assembly in Acidithiobacillus ferrooxidans. In this study the gene of IscS from Aferrooxidans ATCC 23270 was cloned and expressed in Escherichia coli, the protein was purified by one-step affinity chromatography to homogeneity. The molecular mass of recombinant IscS was 46 kDa by SDS-PAGE. The IscS was a pyridoxal phosphate-containing protein, that catalyzed the elimination of S from l-cysteine to yield l-alanine and elemental sulfur or H2S, depending on whether or not a reducing agent was added to the reaction mixture.

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Acknowledgements

This work was supported by the National Basic Research Program of P. R. China (2004CB619204) and National Natural Science Group Foundation of P. R. China (50621063).

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Correspondence to Jianshe Liu.

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Jia Zeng and Yanfei Zhang contributed equally to this work.

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Zeng, J., Zhang, Y., Liu, Y. et al. Expression, purification and characterization of a cysteine desulfurase, IscS, from Acidithiobacillus ferrooxidans . Biotechnol Lett 29, 1983–1990 (2007). https://doi.org/10.1007/s10529-007-9491-6

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  • DOI: https://doi.org/10.1007/s10529-007-9491-6

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