Abstract:
:By proteomic analysis, we found a rhodanese-like protein(RhdA) from Acidithiobacillus ferrooxidans ATCC 23270 whose C-terminal contained a cysteine motif (Cys-XX-Trp-XX-Cys), known to bind iron-sulfur clusters. But so far, there were no articles to confirm the existence of iron-sulfur cluster in RhdA. In this study, RhdA gene from A. ferrooxidans ATCC 23270 was cloned and expressed in Escherichia coli, the protein was purified by one-step affinity chromatography to homogeneity. The UV-Vis scanning and EPR spectra results indicated that the wild-type proteins contained an iron-sulfur cluster. Site-directed mutagenesis results revealed that the four cysteines Cys92, Cys101, Cys197, and Cys203 were crucial residues for iron-sulfur cluster binding.
journal_name
Curr Microbioljournal_title
Current microbiologyauthors
Dai Y,Liu J,Zheng C,Wu A,Zeng J,Qiu Gdoi
10.1007/s00284-009-9476-xsubject
Has Abstractpub_date
2009-11-01 00:00:00pages
559-64issue
5eissn
0343-8651issn
1432-0991journal_volume
59pub_type
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