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

Angew Chem Int Ed Engl. 2021 Jun 14;60(25):13824-13828. doi: 10.1002/anie.202101186. Epub 2021 May 11.

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.

Keywords: asymmetric catalysis; biocatalysis; cofactor recycling; ene-reductase; hydrogenation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alkenes / chemistry
  • Alkenes / metabolism*
  • Biocatalysis
  • Escherichia coli / enzymology*
  • Flavins / chemistry
  • Flavins / metabolism*
  • Hydrogenase / chemistry
  • Hydrogenase / metabolism*
  • Hydrogenation
  • Molecular Structure
  • Oxidation-Reduction
  • Oxidoreductases / chemistry
  • Oxidoreductases / metabolism*

Substances

  • Alkenes
  • Flavins
  • Oxidoreductases
  • nickel-iron hydrogenase
  • Hydrogenase