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Updated: Mar 12, 2026

Scale-up Chemical Synthesis of Thermally-activated Delayed Fluorescence Emitters Based on the Dibenzothiophene-S,S-Dioxide Core
Published on: October 24, 2017
Initial investigations of C4a-(hydro)peroxyflavin intermediate formation by dibenzothiophene monooxygenase
Liliana Gonzalez-Osorio1, Kelvin Luong1, Samatar Jirde1
1Department of Chemistry and Biochemistry, California State University, Northridge, Northridge, CA 91330-8262, United States.
Abstract:
Dibenzothiophene monooxygenase is the initiating enzyme in the Rhodococcus 4S biodesulfurization pathway. A member of the Class D flavin monooxygenases, it uses FMN to activate molecular oxygen for oxygenation of the substrate, dibenzothiophene. Here, we have used stopped-flow spectrophotometry to show that DszC forms a peroxyflavin intermediate in the absence of substrate. Mutagenesis of Ser163 and His391 to Ala appears to decrease the binding affinity for reduced FMN and eliminates the enzyme's ability to stabilize the peroxyflavin intermediate.
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