Crystal structure of the flavoprotein ArsH from Sinorhizobium meliloti

Jun Ye, Hung Chi Yang, Barry P. Rosen*, Hiranmoy Bhattacharjee

*Corresponding author for this work

Research output: Contribution to journalJournal Article peer-review

56 Scopus citations

Abstract

Purified ArsH from Sinorhizobium meliloti exhibits NADPH:FMN-dependent reduction of molecular O2 to hydrogen peroxide and catalyzes reduction of azo dyes. The structure of ArsH was determined at 1.8 Å resolution. ArsH crystallizes with eight molecules in the asymmetric unit forming two tetramers. Each monomer has a core domain with a central five-stranded parallel β-sheet and two monomers interact to form a classical flavodoxin-like dimer. The N- and C-terminal extensions of ArsH are involved in interactions between subunits and tetramer formation. The structure may provide insight in how ArsH participates in arsenic detoxification.

Original languageEnglish
Pages (from-to)3996-4000
Number of pages5
JournalFEBS Letters
Volume581
Issue number21
DOIs
StatePublished - 21 08 2007
Externally publishedYes

Keywords

  • ArsH
  • Arsenic detoxification
  • Azoreductase
  • Flavoprotein
  • NADPH-FMN oxidoreductase

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