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- W2912234990 abstract "On the basis of its catalytic promiscuity, wild-type myoglobin (Mb) from horse heart was used for in situ regeneration of oxidized nicotinamide cofactors. Mb proved to be a versatile catalyst, since it was capable of efficient oxidation of both natural cofactors NAD(P)H and their synthetic biomimetic BNAH with H2O2. Mb-catalyzed oxidation of reduced nicotinamide cofactors was promoted significantly in the presence of mediators such as scopoletin and acetaminophen. A cofactor total turnover number (TTN) up to 50 000 was obtained in glucose dehydrogenase-catalyzed oxidation of glucose coupled with the Mb/scopoletin regeneration system. Approximately 4 mol of glucose was enzymatically oxidized with 1 mol of H2O2. Besides, this system is well compatible with various dehydrogenases. The desired products were afforded with yields of 93–97% in dehydrogenase-catalyzed oxidations. A radical mechanism was proposed for Mb/scopoletin-catalyzed recycling of NAD(P)+. The Mb-based recycling system may create opportunities for academic and industrial biocatalytic applications." @default.
- W2912234990 created "2019-02-21" @default.
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- W2912234990 date "2019-02-01" @default.
- W2912234990 modified "2023-10-17" @default.
- W2912234990 title "Myoglobin-Catalyzed Efficient In Situ Regeneration of NAD(P)<sup>+</sup> and Their Synthetic Biomimetic for Dehydrogenase-Mediated Oxidations" @default.
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- W2912234990 doi "https://doi.org/10.1021/acscatal.8b04890" @default.
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