Phenylarsonic acid is the parent compound of a group of derivatives that occur as anthropogenic environmental contaminants in both less toxic As(V) and much more toxic As(III) redox states. To elucidate the mechanisms underlying their enzymatic redox conversions, the activities of two flavin reductases, ArsH and FerA, from the soil bacterium Paracoccus denitrificans were compared. The stopped-flow data demonstrated that PhAs(V) oxidized dihydroflavin mononucleotide bound to ArsH, but not to FerA. This result proves that ArsH has some substrate specificity for organoarsenic compounds. Under aerobic conditions, both enzymes accelerated the oxidation of PhAs(III) in a catalase-sensitive manner, indicating that hydrogen peroxide acts as an intermediate. H2O2 was shown to react with PhAs(III) in a bimolecular (1:1) irreversible reaction. When exposed to blue light, flavin alone mediated rapid oxidation of PhAs(III) by O2. Photooxidation by flavin acted in concert with chemical oxidation by transiently accumulating H2O2. The described processes may be relevant in the context of arsenic ecotoxicology and remediation.

Department of Biochemistry Faculty of Science Masaryk University Kotlářská 267 2 61137 Brno Czech Republic

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