Please use this identifier to cite or link to this item: http://dx.doi.org/10.25673/111373
Title: Light-controlled biocatalysis by unspecific peroxygenases with genetically encoded photosensitizers
Author(s): Püllmann, PascalLook up in the Integrated Authority File of the German National Library
Homann, Dominik
Karl, Tobias A.
König, BurkhardLook up in the Integrated Authority File of the German National Library
Weissenborn, Martin J.
Issue Date: 2023
Type: Article
Language: English
Abstract: Fungal unspecific peroxygenases (UPOs) have gained substantial attention for their versatile oxyfunctionalization chemistry paired with impressive catalytic capabilities. A major drawback, however, remains their sensitivity towards their co-substrate hydrogen peroxide, necessitating the use of smart in situ hydrogen peroxide generation methods to enable efficient catalysis setups. Herein, we introduce flavin-containing protein photosensitizers as a new general tool for light-controlled in situ hydrogen peroxide production. By genetically fusing flavin binding fluorescent proteins and UPOs, we have created two virtually self-sufficient photo-enzymes (PhotUPO). Subsequent testing of a versatile substrate panel with the two divergent PhotUPOs revealed two stereoselective conversions. The catalytic performance of the fusion protein was optimized through enzyme and substrate loading variation, enabling up to 24300 turnover numbers (TONs) for the sulfoxidation of methyl phenyl sulfide. The PhotUPO concept was upscaled to a 100 mg substrate preparative scale, enabling the extraction of enantiomerically pure alcohol products.
URI: https://opendata.uni-halle.de//handle/1981185920/113327
http://dx.doi.org/10.25673/111373
Open Access: Open access publication
License: (CC BY-NC 4.0) Creative Commons Attribution NonCommercial 4.0(CC BY-NC 4.0) Creative Commons Attribution NonCommercial 4.0
Journal Title: Angewandte Chemie
Publisher: Wiley-VCH
Publisher Place: Weinheim
Volume: 135
Issue: 41
Original Publication: 10.1002/ange.202307897
Page Start: 1
Page End: 9
Appears in Collections:Open Access Publikationen der MLU