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Complete Enzymatic Oxidation of Methanol to Carbon Dioxide: Towards More Eco‐Efficient Regeneration Systems for Reduced Nicotinamide Cofactors
Author(s) -
Kara Selin,
Schrittwieser Joerg H.,
Gargiulo Serena,
Ni Yan,
Yanase Hideshi,
Opperman Diederik J.,
van Berkel Willem J. H.,
Hollmann Frank
Publication year - 2015
Publication title -
advanced synthesis and catalysis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.541
H-Index - 155
eISSN - 1615-4169
pISSN - 1615-4150
DOI - 10.1002/adsc.201500173
Subject(s) - chemistry , cofactor , methanol , formate dehydrogenase , alcohol dehydrogenase , formate , formaldehyde dehydrogenase , nicotinamide , nad+ kinase , monooxygenase , catalysis , hydroxylation , alcohol , organic chemistry , enzyme , cytochrome p450
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 (CO 2 ) 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 CC‐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 k cat and high K M value of the ADH used) necessitating higher than theoretical methanol concentrations.