Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2053179 | FEBS Letters | 2005 | 5 Pages |
Abstract
After heterologous expression in Escherichia coli, the Azotobacter vinelandii rhodanese RhdA is purified in a persulfurated form (RhdA-SSH). We identified l-cysteine as the most effective sulfur source in producing RhdA-SSH. An E. coli soluble extract was required for in vitro persulfuration of RhdA, and the addition of pyridoxal-5′-phosphate increased RhdA-SSH production, indicating a likely involvement of a cysteine desulfurase. We were able to show the formation of a covalent complex between IscS and RhdA. By combining a time-course fluorescence assay and mass spectrometry analysis, we demonstrated the transfer of sulfur from E. coli IscS to RhdA.
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Authors
Fabio Forlani, Angelo Cereda, Andrea Freuer, Manfred Nimtz, Silke Leimkühler, Silvia Pagani,