Myoglobin-Catalyzed Efficient In Situ Regeneration of NAD(P)+ and Their Synthetic Biomimetic for Dehydrogenase-Mediated Oxidations
| Autor: | Hao-Yu Jia, Ning Li, Gao-Wei Zheng, Min-Hua Zong |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
Nicotinamide
biology 010405 organic chemistry Dehydrogenase General Chemistry 010402 general chemistry 01 natural sciences Combinatorial chemistry Catalysis Cofactor 0104 chemical sciences Turnover number Enzyme catalysis chemistry.chemical_compound chemistry Myoglobin Scopoletin biology.protein NAD+ kinase |
| Zdroj: | ACS Catalysis. 9:2196-2202 |
| ISSN: | 2155-5435 |
| DOI: | 10.1021/acscatal.8b04890 |
| Popis: | 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 opportuniti... |
| Databáze: | OpenAIRE |
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