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Herein we describe the first representative of an E2-type two-component styrene monooxygenase of proteobacteria. It comprises a single epoxidase protein ( Vp StyA1) and a two domain protein ( Vp StyA2B) harboring an epoxidase (A2) and a FAD-reductase (B) domain. It was annotated as Vp StyA1/ Vp StyA2B of Variovorax paradoxus EPS. Vp StyA2B serves mainly as NADH:FAD-oxidoreductase. A K  m of 33.6 ± 4.0 µM for FAD and a k  cat of 22.3 ± 1.1 s -1 were determined and resulted in a catalytic efficiency ( k  cat  K  m  -1 ) of 0.64 s -1 μM -1 . To investigate its NADH:FAD-oxidoreductase function the linker between A2- and B-domain (AREAV) was mutated. One mutant () showed 18.7-fold higher affinity for FAD ( k  cat  K  m  -1 of 5.21 s -1 μM -1 ) while keeping wildtype NADH-affinity and -oxidation activity. Both components, Vp StyA2B and Vp StyA1, showed monooxygenase activity on styrene of 0.14 U mg -1 and 0.46 U mg -1 , as well as on benzyl methyl sulfide of 1.62 U mg -1 and 3.11 U mg -1 , respectively. The high sulfoxidase activity was the reason to test several thioanisole-like substrates in biotransformations. Vp StyA1 showed high substrate conversions (up to 95% in 2 h) and produced dominantly ( S )-enantiomeric sulfoxides of all tested substrates. The -mutant showed a 1.6-fold increased monooxygenase activity. In comparison, the GQWCSQY-mutant did neither show monooxygenase nor efficient FAD-reductase activity. Hence, the linker between the two domains of Vp StyA2B has effects on the reductase as well as on the monooxygenase performance. Overall, this monooxygenase represents a promising candidate for biocatalyst development and studying natural fusion proteins.

VpStyA1/VpStyA2B of Variovorax paradoxus EPS: An Aryl Alkyl Sulfoxidase Rather than a Styrene Epoxidizing Monooxygenase