C═C-Ene-Reductases Reduce the C═N Bond of Oximes
| Autor: | Florian Hamm, Ronald A. Glabonjat, Wolfgang Kroutil, Willem B. Breukelaar, Stefan Velikogne |
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| Rok vydání: | 2020 |
| Předmět: |
chemistry.chemical_classification
biocatalysis ene-reductases Pyrazine 010405 organic chemistry Stereochemistry General Chemistry 010402 general chemistry Oxime oxime 01 natural sciences humanities Catalysis 0104 chemical sciences chemistry.chemical_compound Enzyme amine chemistry Biocatalysis pyrazine Amine gas treating Ene reaction Research Article |
| Zdroj: | ACS Catalysis |
| ISSN: | 2155-5435 |
| Popis: | Although enzymes have been found for many reactions, there are still transformations for which no enzyme is known. For instance, not a single defined enzyme has been described for the reduction of the C=N bond of an oxime, only whole organisms. Such an enzymatic reduction of an oxime may give access to (chiral) amines. By serendipity, we found that the oxime moiety adjacent to a ketone as well as an ester group can be reduced by ene-reductases (ERs) to an intermediate amino group. ERs are well-known enzymes for the reduction of activated alkenes, as of α,β-unsaturated ketones. For the specific substrate used here, the amine intermediate spontaneously reacts further to tetrasubstituted pyrazines. This reduction reaction represents an unexpected promiscuous activity of ERs expanding the toolkit of transformations using enzymes. |
| Databáze: | OpenAIRE |
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