Complete Enzymatic Oxidation of Methanol to Carbon Dioxide: Towards More Eco‐Efficient Regeneration Systems for Reduced Nicotinamide Cofactors. Issue 8 (29th April 2015)

• Record Type: Journal Article
• Authors: Kara, Selin; Schrittwieser, Joerg H.; Gargiulo, Serena; Ni, Yan; Yanase, Hideshi; Opperman, Diederik J.; van Berkel, Willem J. H.; Hollmann, Frank
• Is Part Of: Advanced synthesis & catalysis. Volume 357:Issue 8(2015)
• Page Start: 1687
• Page End: 1691
• Publication Date: 2015-04-29
• Subjects: Catalysis -- Periodicals; Organic compounds -- Synthesis -- Periodicals; Chemistry -- Periodicals; Chemistry, Technical -- Periodicals; Chemistry -- Periodicals; Catalysis -- Periodicals; Technology, Pharmaceutical -- Periodicals; 547.2
• DOI: 10.1002/adsc.201500173
• Languages: English
• ISSNs: 1615-4150

Abstract

<abstract abstract-type="main" xml:lang="en"> <title>Abstract</title> <p>A novel system for <italic>in situ</italic> 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 <italic>k</italic>_cat and high <italic>K</italic>_M value of the ADH used) necessitating higher than theoretical methanol concentrations.</p> <p> <graphic position="anchor" mimetype="image" xlink:href="ark:/27927/pgjng095nr" orientation="portrait" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" /> </p> </abstract>