Expression, purification and characterization of the sulfite reductase hemo-subunit, SiR-HP, from Acidithiobacillus ferrooxidans

被引：2

作者：

Zeng, Jia ^{[1
]}

Wang, Ming ^{[1
]}

Zhang, Xiaojian ^{[1
]}

Wang, Yiping ^{[1
]}

Ai, Chenbin ^{[1
]}

Liu, Jianshe ^{[1
]}

Qiu, Guanzhou ^{[1
]}

机构：

[1] Cent S Univ, Sch Resources Proc & Bioengn, Dept Bioengn, Changsha 410083, Peoples R China

来源：

BIOTECHNOLOGY LETTERS | 2008年 / 30卷 / 07期

关键词：

Acidithiobacillus ferrooxidans; expression; mutation; purification; sulfite reductase;

D O I：

10.1007/s10529-008-9679-4

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

Sulfite reductase (SiR) is a large and soluble enzyme which catalyzes the transfer of six electrons from NADPH to sulfite to produce sulfide. The sulfite reductase flavoprotein (SiR-FP) contains both FAD and FMN, and the sulfite reductase hemoprotein (SiR-HP) contains an iron-sulfur cluster coupled to a siroheme. The enzyme is arranged so that the redox cofactors in the FAD-FMN-Fe4S4-Heme sequence make an electron pathway between NADPH and sulfite. Here we report the cloning, expression, and characterization of the SiR-HP of the sulfite reductase from Acidithiobacillus ferrooxidans. The purified SiR-HP contained a [Fe4S4] cluster. Site-directed mutagenesis results revealed that Cys427, Cys433, Cys472 and Cys476 were in ligating with the [Fe4S4] cluster of the protein.

引用

页码：1239 / 1244

页数：6

共 25 条

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