The stoichiometry of the dimethyl sulfone (DMSO2) monooxygenase SfnG catalyzed reaction from Pseudomonas fluorescens Pf0-1 has been reported. In the presence of FMN, NADH, and a flavin reductase, The enzyme SfnG converts DMSO2 to methanesulfinate by oxidative cleavage of the C-S bond. However, it is not known if SfnG is only specific for DMSO2 as a substrate. Therefore, the substrate range of the sulfur assimilation enzyme was investigated. In order to verify the function of SfnG in the overall biochemical transformation with other substrates, The His-tagged protein was produced in Escherichia coli in milligram quantities and purified by Ni-affinity chromatography. Purified SfnG was characterized by the teachnique of mass spectrometry. The concentration of SfnG was determined by both a Bradford assay and by Beer’s Law. The enzyme function with diethyl sulfone was tested with 1H NMR spectroscopy via an endpoint assay. Thus, the product of SfnG with diethyl sulfone as a substrate will be reported.

Substrate specificity of the sulfur assimilation enzyme SfnG

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.