Abstract The biological assimilation of dimethylsulfone can be achieved by a series of enzymatic reactions. The enzymes are monooxygenases that require the reduced form of flavin mononucleotide (FMNH2) provided by reduced nicotinamide adenine dinucleotide (NADH)-dependent MsuE. The final step of the pathway is the conversion of methanesulfonate (CH3SO3–) to inorganic sulfite (SO3–) catalyzed by the enzyme MsuD. The homologous enzyme has been reported from Pseudomonas aeruginosa PAO1. The chemical reaction catalyzed by MsuD has also been reported; methanesulfonate, oxygen, and FMNH2 react to produce sulfite, formaldehyde, water, and the oxidized form of flavin mononucleotide (FMN). Milligram quantities of MsuD from the genome of P. fluorescens Pf0-1 were produced in E. coli, purified by nickel affinity chromatography, and quantified by Bradford assay and Beer’s Law. Both MsuD and MsuE were characterized by mass spectrometry.

Production, purification, and quantification of the reduced flavin-dependent monooxygenase MsuD from Pseudomonas fluorescens Pf0-1

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.