Nonenzymatic Regeneration of Styrene Monooxygenase for Catalysis

Research output: Contribution to journalResearch articleContributedpeer-review

Contributors

  • Caroline E. Paul - , Delft University of Technology (Author)
  • Dirk Tischler - , Freiberg University of Mining and Technology (Author)
  • Anika Riedel - , Freiberg University of Mining and Technology (Author)
  • Thomas Heine - , Freiberg University of Mining and Technology (Author)
  • Nobuya Itoh - , Toyama Prefectural University (Author)
  • Frank Hollmann - , Delft University of Technology (Author)

Abstract

Styrene monooxygenase (SMO) is a two-component flavoprotein catalyzing the selective epoxidation of various C=C double bonds. For cell-free catalysis, traditionally a cascade of NAD(P)H:flavin oxidoreductase, nicotinamide cofactor (NADH), and NADH regeneration enzyme is required to supply StyA with the reduced flavin adenine dinucleotide cofactor (FADH2) required for catalysis. Herein, we present a more direct and efficient FADH2 regeneration system using the nicotinamide cofactor mimic 1-benzyl-1,4-dihydronicotinamide (BNAH) as the sole reductant. Thus, BNAH replaces two enzymes and the nicotinamide cofactor, resulting in a significantly simplified reaction system. (Chemical Equation Presented).

Details

Original languageEnglish
Pages (from-to)2961-2965
Number of pages5
JournalACS catalysis
Volume5
Issue number5
Publication statusPublished - 1 May 2015
Peer-reviewedYes
Externally publishedYes

External IDs

ORCID /0000-0002-7109-2788/work/172571679

Keywords

ASJC Scopus subject areas

Keywords

  • asymmetric epoxidation, electron transfer, mNADHs, styrene monooxygenases, two-component flavin monooxygenases