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Assembly mechanism of [Fe2S2] cluster in ferredoxin from Acidithiobacillus ferrooxidans
Qian Chen1, Hongyu Mo, Lin Tang
1Department of Bioengineering, School of Resources Processing and Bioengineering, Central South University, Changsha, Hunan 410083, P. R. China.
Abstract:
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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