1H, 13C and 15N resonance assignments of rhodanese GlpE from Escherichia coli
- 影响因子：
0.0
- 发表刊物：
Biomol. NMR Assign.
- 摘要：
Rhodanese catalyzes the sulfur-transfer reaction in which a sulfur atom is transferred from thiosulfate to cyanide by a double-displacement mechanism. During the reaction, a persulfide-intermediate form of rhodanese is generated by the reaction of a conserved active cysteine residue with thiosulfate. Escherichia coli GlpE is a prototype for the single-domain rhodanese superfamily. Though there are some studies on rhodaneses, the molecular mechanism of the catalytic activity of rhodaneses is still unclear. Herein, we report the resonance assignments of (1)H, (13)C and (15)N atoms of E. coli GlpE, which provides the basis for further structural, dynamic and functional studies of rhodaneses using NMR technique.
- 论文类型：
期刊论文
- 论文编号：
36
- 卷号：
5
- 期号：
1
- 页面范围：
97-99
- 是否译文：
否
- 发表时间：
2011-04-01
- 收录刊物：
SCI
- 发布期刊链接：
- 第一作者：
Li Hongwei
- 通讯作者：
Jin Changwen
- 全部作者：
Xia Bin
