Litcius/Paper detail

<i>E. coli</i> Nickel‐Iron Hydrogenase 1 Catalyses Non‐native Reduction of Flavins: Demonstration for Alkene Hydrogenation by Old Yellow Enzyme Ene‐reductases**

Shiny Joseph Srinivasan, Sarah E. Cleary, Miguel A. Ramirez, Holly A. Reeve, Caroline E. Paul, Kylie A. Vincent

2021Angewandte Chemie International Edition19 citationsDOIOpen Access PDF

Abstract

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 H 2 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 FMNH 2 or FADH 2 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.

Topics & Concepts

Flavin groupAlkeneCofactorTurnover numberChemistryHydrogenaseEnzymeEne reactionNickelCatalysisPhotochemistryStereochemistryBiochemistryOrganic chemistryMetalloenzymes and iron-sulfur proteinsMicrobial Fuel Cells and BioremediationAmmonia Synthesis and Nitrogen Reduction