E. coli Nickel-Iron Hydrogenase 1 Catalyses Non-native Reduction of Flavins

Demonstration for Alkene Hydrogenation by Old Yellow Enzyme Ene-reductases**

Journal article (2021)

Authors

Shiny Joseph Srinivasan University of Oxford
Sarah E. Cleary University of Oxford
Miguel A. Rico-Ramirez University of Oxford
Holly A. Reeve University of Oxford
C.E. Paul BT/Biocatalysis - AS
Kylie A. Vincent University of Oxford
Research Group
BT/Biocatalysis (AS) (TU Delft)
Copyright: © 2021 Shiny Joseph Srinivasan, Sarah E. Cleary, Miguel A. Ramirez, Holly A. Reeve, C.E. Paul, Kylie A. Vincent
DOI: https://doi.org/10.1002/anie.202101186
Hydrogenation Ene-reductase Biocatalysis Asymmetric catalysis Cofactor recycling
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Published Date

2021

Language

English

Faculty

Applied Sciences

Department

BT/Biotechnologie

Research Group

BT/Biocatalysis

Abstract

A new activity for the [NiFe] uptake hydrogenase 1 of Escherichia coli (Hyd1) is presented. Direct reduction of biological flavin cofactors FMN and FAD is achieved using H2 as a simple, completely atom-economical reductant. The robust nature of Hyd1 is exploited for flavin reduction across a broad range of temperatures (25–70 °C) and extended reaction times. The utility of this system as a simple, easy to implement FMNH2 or FADH2 regenerating system is then demonstrated by supplying reduced flavin to Old Yellow Enzyme “ene-reductases” to support asymmetric alkene reductions with up to 100 % conversion. Hyd1 turnover frequencies up to 20.4 min−1 and total turnover numbers up to 20 200 were recorded during flavin recycling.