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 [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.
Zeng
Jia
J
Department of Bioengineering, School of Resources Processing and Bioengineering, Central South University, Changsha, Hunan 410083, PRC. zengjcsu@yahoo.com.cn
Jiang
Huidan
H
Geng
Meimei
M
Wang
Yiping
Y
Zhang
Xiaojian
X
Liu
Jianshe
J
Qiu
Guanzhou
G
D042763:Acidithiobacillus / Q000378:metabolism*; D001426:Bacterial Proteins / Q000378:metabolism*; D058085:Iron Compounds / Q000737:chemistry / Q000378:metabolism*; D007506:Iron-Sulfur Proteins / Q000378:metabolism*; D045322:Photosynthetic Reaction Center Complex Proteins / Q000378:metabolism*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D013057:Spectrum Analysis; D013440:Sulfides / Q000378:metabolism
D001426:Bacterial Proteins; D058085:Iron Compounds; D007506:Iron-Sulfur Proteins; D045322:Photosynthetic Reaction Center Complex Proteins; D013440:Sulfides; C007943:high potential iron-sulfur protein