In Vitro Assembly of [Fe₄S₄] Cluster in High Potential Iron-Sulfur Protein from Acidithiobacillus ferrooxidans

High-potential iron-sulfur protein (HiPIP) has been proposed to be involved in the iron respiratory electron transport chain in Acidithiobacillus ferrooxidans, which contains an [Fe₄S₄] cluster. We report here the assembly of an [Fe₄S₄] cluster in HiPIP from A. ferrooxidans ATCC 23270 in vitro in th...

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Bibliographic Details
Published in:Current microbiology 2008-08, Vol.57 (2), p.161-166
Main Authors: Zeng, Jia, Jiang, Huidan, Geng, Meimei, Wang, Yiping, Zhang, Xiaojian, Liu, Jianshe, Qiu, Guanzhou
Format: Article
Language:English
Subjects:
Acidithiobacillus - metabolism
Acidithiobacillus ferrooxidans
Bacterial Proteins - metabolism
Biomedical and Life Sciences
Biotechnology
desorption
Electron transfer
electron transport chain
Ionization
Iron
Iron Compounds - chemistry
Iron Compounds - metabolism
Iron-Sulfur Proteins - metabolism
Life Sciences
Mass spectrometry
Microbiology
Photosynthetic Reaction Center Complex Proteins - metabolism
Proteins
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Spectrum Analysis
Sulfides - metabolism
Sulfur
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Summary:High-potential iron-sulfur protein (HiPIP) has been proposed to be involved in the iron respiratory electron transport chain in Acidithiobacillus ferrooxidans, which contains an [Fe₄S₄] cluster. We report here the assembly of an [Fe₄S₄] cluster in HiPIP from A. ferrooxidans ATCC 23270 in vitro in the presence of Fe²⁺ and sulfide. The spectra and matrix-assisted laser desorption ionization-time of flight mass spectrometry results of holoHiPIP confirmed that the iron-sulfur cluster was correctly assembled into the protein.
ISSN:0343-8651
1432-0991
DOI:10.1007/s00284-008-9170-4