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 1.8A 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 beta-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.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Arsenic / metabolism
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Bacterial Proteins / chemistry*
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Bacterial Proteins / metabolism
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Biodegradation, Environmental
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Crystallography, X-Ray
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Drug Resistance, Bacterial / physiology
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Flavin Mononucleotide / metabolism
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Flavoproteins / chemistry*
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Flavoproteins / metabolism
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Hydrogen Peroxide / metabolism
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Industrial Waste
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NADP / metabolism
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Oxidation-Reduction
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Oxidoreductases / chemistry*
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Oxidoreductases / metabolism
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Oxygen / metabolism
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Protein Structure, Tertiary / physiology
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Sinorhizobium meliloti / enzymology*
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Water Pollutants, Chemical / metabolism
Substances
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Bacterial Proteins
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Flavoproteins
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Industrial Waste
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Water Pollutants, Chemical
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NADP
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Flavin Mononucleotide
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Hydrogen Peroxide
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Oxidoreductases
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Arsenic
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Oxygen