4.8 Article

C=C-Ene-Reductases Reduce the C=N Bond of Oximes

Journal

ACS CATALYSIS
Volume 10, Issue 22, Pages 13377-13382

Publisher

AMER CHEMICAL SOC
DOI: 10.1021/acscatal.0c03755

Keywords

biocatalysis; ene-reductases; oxime; amine; pyrazine

Funding

  1. BMVIT
  2. BMDW
  3. SFG
  4. Standortagentur Tirol
  5. Government of Lower Austria und Vienna Business Agency of COMET-Competence Centers for Excellent Technologies
  6. University of Graz
  7. Doctoral Academy
  8. Field of Excellence BioHealth
  9. NAWI-Graz
  10. Austrian Science Fund (FWF) [DOC 46-821]

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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 alpha,beta-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.

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