Asp97 is a crucial residue involved in the ligation of the [Fe₄S₄] cluster of IscA from Acidithiobacillus ferrooxidans

IscA was proposed to be involved in the iron-sulfur cluster assembly encoded by the iscSUA operon, but the role of IscA in the iron-sulfur cluster assembly still remains controversial. In our previous study, the IscA from A. ferrooxidans was successfully expressed in Escherichia coli, and purified t...

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Veröffentlicht in:Journal of microbiology and biotechnology 2008-06, Vol.18 (6), p.1070-1075
Hauptverfasser: Jiang, Huidan (Central South University, Changsha, P. R. China), Zhang, Xiaojian (Central South University, Changsha, P. R. China), Ai, Chenbing (Central South University, Changsha, P. R. China), Liu, Yuandong (Central South University, Changsha, P. R. China), Liu, Jianshe (Central South University, Changsha, P. R. China), Qiu, Guanzhou (Central South University, Changsha, P. R. China), Zeng, Jia (Central South University, Changsha, P. R. China), E-mail: csuzengjia@yahoo.com.cn
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Zusammenfassung:IscA was proposed to be involved in the iron-sulfur cluster assembly encoded by the iscSUA operon, but the role of IscA in the iron-sulfur cluster assembly still remains controversial. In our previous study, the IscA from A. ferrooxidans was successfully expressed in Escherichia coli, and purified to be a [Fe₄S₄]-cluster-containing protein. Cys35, Cys99, and Cys101 were important residues in ligating with the [Fe₄S₄] cluster. In this study, Asp97 was found to be another ligand for the iron-sulfur cluster binding according to site-directed mutagenesis results. Molecular modeling for the IscA also showed that Asp97 was a strong ligand with the [Fe₄S₄] cluster, which was in good agreement with the experimental results. Thus, the [Fe₄S₄] cluster in IscA from A. ferrooxidans was ligated by three cysteine residues and one aspartic acid.
ISSN:1017-7825