Details
| Original language | English |
|---|---|
| Pages (from-to) | 1687-1691 |
| Number of pages | 5 |
| Journal | Advanced Synthesis and Catalysis |
| Volume | 357 |
| Issue number | 8 |
| Early online date | 29 Apr 2015 |
| Publication status | Published - 26 May 2015 |
| Externally published | Yes |
Abstract
A novel system for in situ regeneration of reduced nicotinamide cofactors (NADH) is proposed: through a cascade of alcohol dehydrogenase (ADH), formaldehyde dismutase (FDM) and formate dehydrogenase (FDH) complete oxidation of methanol to carbon dioxide (CO2) is coupled to the regeneration of NADH. As a consequence, from one equivalent of methanol three equivalents of NADH can be obtained. The feasibility of this cascade is demonstrated at the examples of an NADH-dependent reduction of conjugated C=C-double bonds (catalysed by an enoate reductase) and the NADH-dependent hydroxylation of phenols (catalysed by a monooxygenase). The major limitation of the current regeneration system is the comparably poor catalytic efficiency of the methanol oxidation step (low kcat and high KM value of the ADH used) necessitating higher than theoretical methanol concentrations.
Keywords
- cofactor regeneration, complete methanol oxidation, enzymatic cascades, oxidoreductases
ASJC Scopus subject areas
- Chemical Engineering(all)
- Catalysis
- Chemistry(all)
- Organic Chemistry
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In: Advanced Synthesis and Catalysis, Vol. 357, No. 8, 26.05.2015, p. 1687-1691.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Complete Enzymatic Oxidation of Methanol to Carbon Dioxide
T2 - Towards More Eco-Efficient Regeneration Systems for Reduced Nicotinamide Cofactors
AU - Kara, Selin
AU - Schrittwieser, Joerg H.
AU - Gargiulo, Serena
AU - Ni, Yan
AU - Yanase, Hideshi
AU - Opperman, Diederik J.
AU - Van Berkel, Willem J.H.
AU - Hollmann, Frank
PY - 2015/5/26
Y1 - 2015/5/26
N2 - A novel system for in situ regeneration of reduced nicotinamide cofactors (NADH) is proposed: through a cascade of alcohol dehydrogenase (ADH), formaldehyde dismutase (FDM) and formate dehydrogenase (FDH) complete oxidation of methanol to carbon dioxide (CO2) is coupled to the regeneration of NADH. As a consequence, from one equivalent of methanol three equivalents of NADH can be obtained. The feasibility of this cascade is demonstrated at the examples of an NADH-dependent reduction of conjugated C=C-double bonds (catalysed by an enoate reductase) and the NADH-dependent hydroxylation of phenols (catalysed by a monooxygenase). The major limitation of the current regeneration system is the comparably poor catalytic efficiency of the methanol oxidation step (low kcat and high KM value of the ADH used) necessitating higher than theoretical methanol concentrations.
AB - A novel system for in situ regeneration of reduced nicotinamide cofactors (NADH) is proposed: through a cascade of alcohol dehydrogenase (ADH), formaldehyde dismutase (FDM) and formate dehydrogenase (FDH) complete oxidation of methanol to carbon dioxide (CO2) is coupled to the regeneration of NADH. As a consequence, from one equivalent of methanol three equivalents of NADH can be obtained. The feasibility of this cascade is demonstrated at the examples of an NADH-dependent reduction of conjugated C=C-double bonds (catalysed by an enoate reductase) and the NADH-dependent hydroxylation of phenols (catalysed by a monooxygenase). The major limitation of the current regeneration system is the comparably poor catalytic efficiency of the methanol oxidation step (low kcat and high KM value of the ADH used) necessitating higher than theoretical methanol concentrations.
KW - cofactor regeneration
KW - complete methanol oxidation
KW - enzymatic cascades
KW - oxidoreductases
UR - http://www.scopus.com/inward/record.url?scp=85027924625&partnerID=8YFLogxK
U2 - 10.1002/adsc.201500173
DO - 10.1002/adsc.201500173
M3 - Article
AN - SCOPUS:85027924625
VL - 357
SP - 1687
EP - 1691
JO - Advanced Synthesis and Catalysis
JF - Advanced Synthesis and Catalysis
SN - 1615-4150
IS - 8
ER -