We found a match
Your institution may have rights to this item. Sign in to continue.
- Title
Expression, purification and characterization of a cysteine desulfurase, IscS, from Acidithiobacillus ferrooxidans.
- Authors
Jia Zeng; Yanfei Zhang; Yuandong Liu; Xiaojian Zhang; Leixian Xia; Jianshe Liu; Guanzhou Qiu
- 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 H2S, depending on whether or not a reducing agent was added to the reaction mixture.
- Subjects
METAL clusters; GENE expression; CYSTATHIONINE gamma-lyase; CHROMATOGRAPHIC analysis; ESCHERICHIA coli; RECOMBINANT proteins; LYASES; MOLECULAR cloning; ESCHERICHIA
- Publication
Biotechnology Letters, 2007, Vol 29, Issue 12, p1983
- ISSN
0141-5492
- Publication type
Article
- DOI
10.1007/s10529-007-9491-6