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H-1, C-13 and N-15 resonance assignments of the arsenate reductase from Synechocystis sp strain PCC 6803
Yu, Caifang ; Xia, Bin ; Jin, Changwen
刊名biomolecular nmr assignments
2011
关键词ArsC Arsenate reductase Assignments NMR Enzyme IDENTIFICATION DETOXIFICATION MECHANISM PROTEINS CASCADE SYSTEM
DOI10.1007/s12104-010-9273-2
英文摘要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 H-1, C-13 and N-15 atoms for the reduced form of SynArsC, which provides a starting point for further structural analysis and elucidation of its enzymatic mechanism.; Biophysics; Spectroscopy; SCI(E); PubMed; 2; ARTICLE; 1; 85-87; 5
语种英语
内容类型期刊论文
源URL[http://ir.pku.edu.cn/handle/20.500.11897/150045]  
专题化学与分子工程学院
生命科学学院
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GB/T 7714
Yu, Caifang,Xia, Bin,Jin, Changwen. H-1, C-13 and N-15 resonance assignments of the arsenate reductase from Synechocystis sp strain PCC 6803[J]. biomolecular nmr assignments,2011.
APA Yu, Caifang,Xia, Bin,&Jin, Changwen.(2011).H-1, C-13 and N-15 resonance assignments of the arsenate reductase from Synechocystis sp strain PCC 6803.biomolecular nmr assignments.
MLA Yu, Caifang,et al."H-1, C-13 and N-15 resonance assignments of the arsenate reductase from Synechocystis sp strain PCC 6803".biomolecular nmr assignments (2011).
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