Hybrid catalysis for enantioselective Baeyer-Villiger oxidation and stereoselective epoxidation: a Cp*Ir complex to fuel FMN and FAD reduction for flavoprotein monooxygenase modules

Taking advantage of the unique properties of two-component flavo-monooxygenases and the ability of [Cp*Ir(bpy-OMe)H]⁺ to transfer hydrides to reduce flavins, we extended the scope of the pH- and oxygen-robust iridium(iii)-complex to drive the enzymatic reaction of a FMN-dependent Baeyer-Villiger monooxygenase and a FAD-dependent...

Exploring the Temperature Effect on Enantioselectivity of a Baeyer-Villiger Biooxidation by the 2,5-DKCMO Module: The SLM Approach

Temperature is a crucial parameter for biological and chemical processes. Its effect on enzymatically catalysed reactions has been known for decades, and stereo- and enantiopreference are often temperature-dependent. For the first time, we present the temperature effect on the Baeyer-Villiger oxidation of rac-bicyclo[3.2.0]hept-2-en-6-one by...

Divorce in the two-component BVMO family: the single oxygenase for enantioselective chemo-enzymatic Baeyer-Villiger oxidations dagger: The single oxygenase for enantioselective chemo-enzymatic Baeyer-Villiger oxidations

Two-component flavoprotein monooxygenases consist of a reductase and an oxygenase enzyme. The proof of functionality of the latter without its counterpart as well as the mechanism of flavin transfer remains unanswered beyond doubt. To tackle this question, we utilized a reductase-free reaction system applying purified 2,5-diketocamphane...