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KMID : 0545120110210020124
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Journal of Microbiology and Biotechnology
2011 Volume.21 No. 2 p.124 ~ p.128
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Assembly Mechanism of [Fe2S2] Cluster in Ferredoxin from Acidithiobacillus ferrooxidans
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Qian Chen
Hongyu Mo
Lin Tang
Juan Du
Fang Qin
Jia Zeng
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Abstract
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Ferredoxin is a typical iron-sulfur protein that is ubiquitous in biological redox systems. This study investigates the in vitro assembly of a [Fe2S2] cluster in the ferredoxin from Acidithiobacillus ferrooxidans in the presence of three scaffold proteins: IscA, IscS, and IscU. The spectra and MALDI-TOF MS results for the reconstituted ferredoxin confirm that the iron-sulfur cluster was correctly assembled in the protein. The inactivation of cysteine desulfurase by L-allylglycine completely blocked any [Fe2S2] cluster assembly in the ferredoxin in E. coli, confirming that cysteine desulfurase is an essential component for iron-sulfur cluster assembly. The present results also provide strong evidence that [Fe2S2] cluster assembly in ferredoxin follows the AUS pathway.
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KEYWORD
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Acidithiobacillus ferrooxidans, ferredoxin, iron-sulfur cluster, assembly
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