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Title of Journal: Curr Microbiol

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Abbravation: Current Microbiology

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Springer-Verlag

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DOI

10.1002/qua.20690

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1432-0991

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Characterization and Reconstitute of a FeSubscri

Authors: Chunli Zheng Yanfei Zhang Yuandong Liu Anna Wu Lexian Xia Jia Zeng Jianshe Liu Guanzhou Qiu
Publish Date: 2009/02/19
Volume: 58, Issue: 6, Pages: 586-
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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 onestep affinity chromatography to apparent homogeneity The molecular mass of the recombinant APS reductase was determined to be 28 kDa using SDSPAGE 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 Sitedirected 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

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