In vitro assembly of [Fe4S4] cluster in high potential iron-sulfur protein from Acidithiobacillus ferrooxidans

Jia Zeng; Huidan Jiang; Meimei Geng; Yiping Wang; Xiaojian Zhang; Jianshe Liu; Guanzhou Qiu

doi:10.1007/s00284-008-9170-4

In vitro assembly of [Fe4S4] cluster in high potential iron-sulfur protein from Acidithiobacillus ferrooxidans

Curr Microbiol. 2008 Aug;57(2):161-6. doi: 10.1007/s00284-008-9170-4. Epub 2008 Jun 24.

Authors

Jia Zeng¹, Huidan Jiang, Meimei Geng, Yiping Wang, Xiaojian Zhang, Jianshe Liu, Guanzhou Qiu

Affiliation

¹ Department of Bioengineering, School of Resources Processing and Bioengineering, Central South University, Changsha, Hunan 410083, PRC. [email protected]

PMID: 18574631
DOI: 10.1007/s00284-008-9170-4

Abstract

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 [Fe(4)S(4)] cluster. We report here the assembly of an [Fe(4)S(4)] cluster in HiPIP from A. ferrooxidans ATCC 23270 in vitro in the presence of Fe(2+) 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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Acidithiobacillus / metabolism*
Bacterial Proteins / metabolism*
Iron Compounds / chemistry
Iron Compounds / metabolism*
Iron-Sulfur Proteins / metabolism*
Photosynthetic Reaction Center Complex Proteins / metabolism*
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Spectrum Analysis
Sulfides / metabolism

Substances

Bacterial Proteins
Iron Compounds
Iron-Sulfur Proteins
Photosynthetic Reaction Center Complex Proteins
Sulfides
high potential iron-sulfur protein