Abstract
Two-component-diffusible-flavomonooxygenases are versatile biocatalysts for selective epoxidation-, hydroxylation- or halogenation reactions. Their complicated molecular architecture can be simplified using photochemical regeneration of the catalytically active, reduced FADH2 prosthetic group. In this contribution we provide the proof-of-concept and characterization for the direct regeneration of the styrene monooxygenase from Pseudomonas.
Highlights
Two-component-diffusible-flavomonooxygenases are versatile biocatalysts for selective epoxidation, hydroxylation- or halogenation reactions. Their complicated molecular architecture can be simplified using photochemical regeneration of the catalytically active, reduced FADH2 prosthetic group. In this contribution we provide the proof-of-concept and characterization for the direct regeneration of the styrene monooxygenase from Pseudomonas
2CDFMOs rely on the reductive activation of molecular oxygen mediated by an enzyme-bound, reduced flavin cofactor
There is an ongoing debate on the mechanism on how FADH2 reaches the monooxygenase subunit
Summary
Two-component-diffusible-flavomonooxygenases are versatile biocatalysts for selective epoxidation-, hydroxylation- or halogenation reactions. Some studies suggest a freely diffusible FADH25 while others found indications for a complex between the reductase- and monooxygenase subunits thereby channelling the reduced flavin and protecting it from spontaneous aerobic reoxidation.[6,7,8] The complicated molecular architecture of 2CDFMOs poses a challenge for their preparative application, which is mostly addressed by whole-cell systems.[9,10,11,12] More recently, fusion proteins combining the reductase- and monooxygenase subunits in one polypeptide chain are moving into the research focus.[13,14] Reactions utilising isolated enzymes require the entire cascade outlined in Scheme 1.15–17 it is no surprise that alternative, more direct and simple regeneration systems for the reduced flavin cofactor have been evaluated.
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