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

Research output: Contribution to journalArticleResearchpeer review

Authors

  • Robert Röllig
  • Caroline E. Paul
  • Pierre Rousselot-Pailley
  • Selin Kara
  • Véronique Alphand

Research Organisations

External Research Organisations

  • Universite d'Aix-Marseille
  • Delft University of Technology
  • Aarhus University
View graph of relations

Details

Original languageEnglish
Pages (from-to)3117-3123
Number of pages7
JournalReaction Chemistry & Engineering
Volume8
Issue number12
Early online date4 Aug 2023
Publication statusPublished - 2023

Abstract

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 styrene monooxygenase (respectively FPMO Group C and E), using formic acid as H-donor for NADH recycling.

Cite this

Hybrid catalysis for enantioselective Baeyer–Villiger oxidation and stereoselective epoxidation: a Cp*Ir complex to fuel FMN and FAD reduction for flavoprotein monooxygenase modules. / Röllig, Robert; Paul, Caroline E.; Rousselot-Pailley, Pierre et al.
In: Reaction Chemistry & Engineering, Vol. 8, No. 12, 2023, p. 3117-3123.

Research output: Contribution to journalArticleResearchpeer review

Röllig R, Paul CE, Rousselot-Pailley P, Kara S, Alphand V. Hybrid catalysis for enantioselective Baeyer–Villiger oxidation and stereoselective epoxidation: a Cp*Ir complex to fuel FMN and FAD reduction for flavoprotein monooxygenase modules. Reaction Chemistry & Engineering. 2023;8(12):3117-3123. Epub 2023 Aug 4. doi: 10.1039/d3re00411b
Röllig, Robert ; Paul, Caroline E. ; Rousselot-Pailley, Pierre et al. / Hybrid catalysis for enantioselective Baeyer–Villiger oxidation and stereoselective epoxidation : a Cp*Ir complex to fuel FMN and FAD reduction for flavoprotein monooxygenase modules. In: Reaction Chemistry & Engineering. 2023 ; Vol. 8, No. 12. pp. 3117-3123.
Download
@article{d171898351624b0e8cf84446dd43ec8e,
title = "Hybrid catalysis for enantioselective Baeyer–Villiger oxidation and stereoselective epoxidation: a Cp*Ir complex to fuel FMN and FAD reduction for flavoprotein monooxygenase modules",
abstract = "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 styrene monooxygenase (respectively FPMO Group C and E), using formic acid as H-donor for NADH recycling.",
author = "Robert R{\"o}llig and Paul, {Caroline E.} and Pierre Rousselot-Pailley and Selin Kara and V{\'e}ronique Alphand",
note = "Funding Information: The authors acknowledge funding from the European Union's Horizon 2020 MSCA ITN-EJD program under grant agreement No. 764920. They thank Prof. Dr D. Tischler for the plasmid bearing the SfStyA gene and Dr K. Duquesne for the plasmid bearing the 2,5-DKCMO gene.",
year = "2023",
doi = "10.1039/d3re00411b",
language = "English",
volume = "8",
pages = "3117--3123",
number = "12",

}

Download

TY - JOUR

T1 - Hybrid catalysis for enantioselective Baeyer–Villiger oxidation and stereoselective epoxidation

T2 - a Cp*Ir complex to fuel FMN and FAD reduction for flavoprotein monooxygenase modules

AU - Röllig, Robert

AU - Paul, Caroline E.

AU - Rousselot-Pailley, Pierre

AU - Kara, Selin

AU - Alphand, Véronique

N1 - Funding Information: The authors acknowledge funding from the European Union's Horizon 2020 MSCA ITN-EJD program under grant agreement No. 764920. They thank Prof. Dr D. Tischler for the plasmid bearing the SfStyA gene and Dr K. Duquesne for the plasmid bearing the 2,5-DKCMO gene.

PY - 2023

Y1 - 2023

N2 - 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 styrene monooxygenase (respectively FPMO Group C and E), using formic acid as H-donor for NADH recycling.

AB - 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 styrene monooxygenase (respectively FPMO Group C and E), using formic acid as H-donor for NADH recycling.

UR - http://www.scopus.com/inward/record.url?scp=85170659033&partnerID=8YFLogxK

U2 - 10.1039/d3re00411b

DO - 10.1039/d3re00411b

M3 - Article

VL - 8

SP - 3117

EP - 3123

JO - Reaction Chemistry & Engineering

JF - Reaction Chemistry & Engineering

IS - 12

ER -

By the same author(s)