Abstract：
:Adenosine 5'-phosphosulfate (APS) reductase is a key enzyme involved in the pathways of sulfate reduction and sulfide oxidation in the biological sulfur cycle. In this study, the gene of APS reductase from Acidithiobacillus ferrooxidans was cloned and expressed in Escherichia coli, the soluble protein was purified by one-step affinity chromatography to apparent homogeneity. The molecular mass of the recombinant APS reductase was determined to be 28 kDa using SDS-PAGE. According to optical and EPR spectra results of the recombinant protein confirmed that the iron-sulfur cluster inserted into the active site of the protein. Site-directed mutation for the enzyme revealed that Cys110, Cys111, Cys193, and Cys196 were in ligation with the iron-sulfur cluster. The [Fe4S4] cluster could be assembled in vitro, and exhibited electron transport and redox catalysis properties. As we know so far, this is the first report of expression in E. coli of APS reductase from A. ferrooxidans.
journal_name
Curr Microbioljournal_title
Current microbiologyauthors
Zheng C,Zhang Y,Liu Y,Wu A,Xia L,Zeng J,Liu J,Qiu Gdoi
10.1007/s00284-009-9375-1subject
Has Abstractpub_date
2009-06-01 00:00:00pages
586-92issue
6eissn
0343-8651issn
1432-0991journal_volume
58pub_type
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