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

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Zeng J, Zhang Y, Liu Y, Zhang X, Xia L, Liu J, Qiu G

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

Biotechnol Lett. 2007 Dec;29(12):1983-90. Epub 2007 Jul 28.

PubMed ID
17660944 [ View in PubMed
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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 A. ferrooxidans 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 H(2)S, depending on whether or not a reducing agent was added to the reaction mixture.

DrugBank Data that Cites this Article

Drug Targets
DrugTargetKindOrganismPharmacological ActionActions
AlanineCysteine desulfurase, mitochondrialProteinHumans
Unknown
Not AvailableDetails