title: Expression, purification and molecular structure modeling of thioredoxin (Trx) and thioredoxin reductase (TrxR) from Acidithiobacillus ferrooxidans.
abstract: 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.
authors.affiliation: Department of Bioengineering, School of Resources Processing and Bioengineering, Central South University, Changsha, Hunan, People's Republic of China.
authors.forename: Yiping
authors.initials: Y
authors.lastname: Wang
authors.forename: Xiaojian
authors.initials: X
authors.lastname: Zhang
authors.forename: Qing
authors.initials: Q
authors.lastname: Liu
authors.forename: Chenbing
authors.initials: C
authors.lastname: Ai
authors.forename: Hongyu
authors.initials: H
authors.lastname: Mo
authors.forename: Jia
authors.initials: J
authors.lastname: Zeng