Nonenzymatic Regeneration of Styrene Monooxygenase for Catalysis
Research output: Contribution to journal › Research article › Contributed › peer-review
Contributors
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 language | English |
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Pages (from-to) | 2961-2965 |
Number of pages | 5 |
Journal | ACS catalysis |
Volume | 5 |
Issue number | 5 |
Publication status | Published - 1 May 2015 |
Peer-reviewed | Yes |
Externally published | Yes |
External IDs
ORCID | /0000-0002-7109-2788/work/172571679 |
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Keywords
ASJC Scopus subject areas
Keywords
- asymmetric epoxidation, electron transfer, mNADHs, styrene monooxygenases, two-component flavin monooxygenases