1H, 13C and 15N resonance assignments of the arsenate reductase from Synechocystis sp. strain PCC 6803
- 影响因子：
0.0
- 发表刊物：
Biomol. NMR Assign.
- 摘要：
Arsenate reductases (ArsC) are a group of enzymes that play essential roles in biological arsenic detoxification pathways by catalyzing the intracellular reduction of arsenate to arsenite, which is subsequently extruded from the cells by specific transport systems. The ArsC protein from cyanobacterium Synechocystis sp. strain PCC 6803 (SynArsC) is related to the thioredoxin-dependent ArsC family, but uses the glutathione/glutaredoxin system for arsenate reduction. Therefore, it is classified to a novel thioredoxin/glutaredoxin hybrid arsenate reductase family. Herein we report the chemical shift assignments of (1)H, (13)C and (15)N atoms for the reduced form of SynArsC, which provides a starting point for further structural analysis and elucidation of its enzymatic mechanism.
- 论文类型：
期刊论文
- 论文编号：
37
- 卷号：
5
- 期号：
1
- 页面范围：
85-87
- 是否译文：
否
- 发表时间：
2011-04-05
- 收录刊物：
SCI
- 发布期刊链接：
- 第一作者：
Yu Caifang
- 通讯作者：
Jin Changwen
- 全部作者：
Xia Bin
