Assembly Mechanism of [Fe2S2] Cluster in Ferredoxin from Acidithiobacillus ferrooxidans

作者：Chen, Qian; Mo, Hongyu; Tang, Lin; Du, Juan; Qin, Fang; Zeng, Jia^*

来源：Journal of Microbiology and Biotechnology, 2011, 21(2): 124-128.

DOI：10.4014/jmb.1005.05025

• Acidithiobacillus ferrooxidans
• ferredoxin
• iron-sulfur cluster
• assembly

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.

• 出版日期2011-2
• 单位湖南大学; 中南大学