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 (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.
journal_name
Biomol NMR Assignjournal_title
Biomolecular NMR assignmentsauthors
Yu C,Xia B,Jin Cdoi
10.1007/s12104-010-9273-2subject
Has Abstractpub_date
2011-04-01 00:00:00pages
85-7issue
1eissn
1874-2718issn
1874-270Xjournal_volume
5pub_type
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