Ontology highlight
ABSTRACT:
SUBMITTER: Messens J
PROVIDER: S-EPMC124290 | biostudies-literature | 2002 Jun
REPOSITORIES: biostudies-literature
Messens Joris J Martins José C JC Van Belle Karolien K Brosens Elke E Desmyter Aline A De Gieter Marjan M Wieruszeski Jean-Michel JM Willem Rudolph R Wyns Lode L Zegers Ingrid I
Proceedings of the National Academy of Sciences of the United States of America 20020618 13
The mechanism of pI258 arsenate reductase (ArsC) catalyzed arsenate reduction, involving its P-loop structural motif and three redox active cysteines, has been unraveled. All essential intermediates are visualized with x-ray crystallography, and NMR is used to map dynamic regions in a key disulfide intermediate. Steady-state kinetics of ArsC mutants gives a view of the crucial residues for catalysis. ArsC combines a phosphatase-like nucleophilic displacement reaction with a unique intramolecular ...[more]