Assembly mechanism of [Fe2S2] cluster in ferredoxin from Acidithiobacillus ferrooxidans |
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| Authors: | Chen Qian Mo Hongyu Tang Lin Du Juan Qin Fang Zeng Jia |
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| Institution: | Department of Bioengineering, School of Resources Processing and Bioengineering, Central South University, Changsha, Hunan 410083, P. R. China. |
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| 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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