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Research article

J. Microbiol. Biotechnol. 2011; 21(2): 124-128

Published online February 28, 2011 https://doi.org/10.4014/jmb.1005.05025

Copyright © The Korean Society for Microbiology and Biotechnology.

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

Qian Chen 1, Hongyu Mo 1, Lin Tang 2, Juan Du 2, Fang Qin 2 and Jia Zeng 1, 2*

1Department of Bioengineering, School of Resources Processing and Bioengineering, Central South University, Changsha, Hunan 410083, P. R. China, 2Center for Biomedical Engineering, Hunan University, Changsha, Hunan 410082, P. R. China

Received: May 17, 2010; Accepted: November 2, 2010

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.

Keywords: Acidithiobacillus ferrooxidans, ferredoxin, iron-sulfur cluster, assembly