Expression, Purification and Molecular Structure Modeling of Thioredoxin (Trx) and Thioredoxin Reductase (TrxR) from Acidithiobacillus ferrooxidans

被引：5
|
作者：
Wang, Yiping [1 ]
Zhang, Xiaojian [1 ]
Liu, Qing [1 ]
Ai, Chenbing [1 ]
Mo, Hongyu [1 ]
Zeng, Jia [1 ,2 ]
机构：
[1] Cent S Univ, Sch Resources Proc & Bioengn, Dept Bioengn, Changsha 410083, Hunan, Peoples R China
[2] Hunan Univ, Ctr Biomed Engn, Changsha 410082, Hunan, Peoples R China
来源：
CURRENT MICROBIOLOGY | 2009年 / 59卷 / 01期
关键词：
Acidithiobacillus ferrooxidans; Molecular structure modeling; Mutation; Thioredoxin; Thioredoxin reductase; ESCHERICHIA-COLI THIOREDOXIN; DISULFIDE; MUTATIONS; OXIDATION; MECHANISM;
D O I：
10.1007/s00284-009-9390-2
中图分类号：
Q93 [微生物学];
学科分类号：
071005 ; 100705 ;
摘要：
The thioredoxin system consists of thioredoxin (Trx), thioredoxin reductase (TrxR) and NADPH, which plays several key roles in maintaining the redox environment of the cell. In Acidithiobacillus ferrooxidans, thioredoxin system may play important functions in the activity regulation of periplasmic proteins and energy metabolism. Here, we cloned thioredoxin (trx) and thioredoxin reductase (trxR) genes from Acidithiobacillus ferrooxidans, and expressed the genes in Escherichia coli. His-Trx and His-TrxR were purified to homogeneity with one-step Ni-NTA affinity column chromatography. Site-directed mutagenesis results confirmed that Cys33, Cys36 of thioredoxin, and Cys142, Cys145 of thioredoxin reductase were active-site residues.
引用
收藏
页码：35 / 41
页数：7
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