Abstract
Sulfite reductase (SiR) is a large and soluble enzyme which catalyzes the transfer of six electrons from NADPH to sulfite to produce sulfide. The sulfite reductase flavoprotein (SiR-FP) contains both FAD and FMN, and the sulfite reductase hemoprotein (SiR-HP) contains an iron–sulfur cluster coupled to a siroheme. The enzyme is arranged so that the redox cofactors in the FAD-FMN-Fe4S4−Heme sequence make an electron pathway between NADPH and sulfite. Here we report the cloning, expression, and characterization of the SiR-HP of the sulfite reductase from Acidithiobacillus ferrooxidans. The purified SiR-HP contained a [Fe4S4] cluster. Site-directed mutagenesis results revealed that Cys427, Cys433, Cys472 and Cys476 were in ligating with the [Fe4S4] cluster of the protein.
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Acknowledgments
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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Zeng, J., Wang, M., Zhang, X. et al. Expression, purification and characterization of the sulfite reductase hemo-subunit, SiR-HP, from Acidithiobacillus ferrooxidans . Biotechnol Lett 30, 1239–1244 (2008). https://doi.org/10.1007/s10529-008-9679-4
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DOI: https://doi.org/10.1007/s10529-008-9679-4