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 language | English |
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Pages (from-to) | 3996-4000 |
Number of pages | 5 |
Journal | FEBS Letters |
Volume | 581 |
Issue number | 21 |
DOIs | |
State | Published - 21 08 2007 |
Externally published | Yes |
Keywords
- ArsH
- Arsenic detoxification
- Azoreductase
- Flavoprotein
- NADPH-FMN oxidoreductase