Abstract
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 1H, 13C and 15N atoms for the reduced form of SynArsC, which provides a starting point for further structural analysis and elucidation of its enzymatic mechanism.
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Acknowledgments
We thank Professor Qingyu Wu (Tsinghua University, China) for providing the Synechocystis sp. strain PCC 6803 cDNA. This work was supported by Grant 2006CB910203 from the National Basic Research Program and Grant 2006AA02A323 from the National High Technology Research and Development Program of China (to C.J.).
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Yu, C., Xia, B. & Jin, C. 1H, 13C and 15N resonance assignments of the arsenate reductase from Synechocystis sp. strain PCC 6803. Biomol NMR Assign 5, 85–87 (2011). https://doi.org/10.1007/s12104-010-9273-2
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DOI: https://doi.org/10.1007/s12104-010-9273-2