Search

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. [ABSTRACT FROM AUTHOR]

The influence of (visible) light on the performance of laccase mediator systems (LMS) was investigated. As a model reaction, LMS-mediated nicotinamide adenine dinucleotide (NAD+) regeneration to promote alcohol dehydrogenase catalyzed oxidation reactions was examined. [ABSTRACT FROM AUTHOR]

Highlights: [•] The structure of the thermophilic NADH-dependent alcohol dehydrogenase has been solved and refined to a resolution of 2.74Å. [•] The structure reveals an absence of peripheral loops and an abundance of salt bridges and hydrogen bonds that are likely to enhance thermostability. [•] A model of the substrate phenylacetone within the TADH active site reveals the basis for (S)-enantioselectivity in the enzyme. [ABSTRACT FROM AUTHOR]