title: Assembly mechanism of [Fe2S2] cluster in ferredoxin from Acidithiobacillus ferrooxidans.
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.
authors.affiliation: Department of Bioengineering, School of Resources Processing and Bioengineering, Central South University, Changsha, Hunan 410083, P. R. China.
authors.forename: Qian
authors.initials: Q
authors.lastname: Chen
authors.forename: Hongyu
authors.initials: H
authors.lastname: Mo
authors.forename: Lin
authors.initials: L
authors.lastname: Tang
authors.forename: Juan
authors.initials: J
authors.lastname: Du
authors.forename: Fang
authors.initials: F
authors.lastname: Qin
authors.forename: Jia
authors.initials: J
authors.lastname: Zeng
mesh_terms: D042763:Acidithiobacillus / Q000378:metabolism*; D013437:Carbon-Sulfur Lyases / Q000235:genetics / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D005288:Ferredoxins / Q000737:chemistry / Q000378:metabolism*; D055786:Gene Knockout Techniques; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
chemical_list: D005288:Ferredoxins; D013437:Carbon-Sulfur Lyases; C080546:cysteine desulfurase