Nicotinamide-independent asymmetric bioreduction of C=C-bonds via disproportionation of enones catalyzed by enoate reductases

• Published in: Tetrahedron Vol. 66; no. 3; pp. 663 - 667
• Main Authors: Stueckler, Clemens, Reiter, Tamara C., Baudendistel, Nina, Faber, Kurt
• Format: Journal Article
• Language: English
• Published: OXFORD Elsevier 16.01.2010
• Subjects: Bioconversions. Hemisynthesis; Biological and medical sciences; Biotechnology; Chemistry; Chemistry, Organic; Exact sciences and technology; Fundamental and applied biological sciences. Psychology; Kinetics and mechanisms; Methods. Procedures. Technologies; Organic chemistry; Physical Sciences; Reactivity and mechanisms; Science & Technology; MECHANISM; PROMISCUITY; disproportionation; CRYSTAL-STRUCTURE; BAEYER-VILLIGER OXIDATION; flavin; OLD YELLOW ENZYME; ELECTROCHEMICAL REGENERATION; enoate reductase; biotransformation; MORPHINONE REDUCTASE; cofactor recycling; MICROBIAL EPOXIDATION; TOMATO; PENTAERYTHRITOL TETRANITRATE REDUCTASE; Flavin derivatives; Hydrogen transfer; Catalytic reaction; Disproportionation; Enzyme; FAD; Diketone; Cofactor recycling; Oxygen heterocycle; Cofactor; Double bond; Chemical reduction; Flavin; Asymmetric synthesis; Enoate reductase; Biotransformation; Oxidoreductases; Recycling; 2-Enoate reductase; Enone
• ISSN: 0040-4020; 1464-5416
• DOI: 10.1016/j.tet.2009.11.065

The asymmetric bioreduction of activated C = C-bonds catalyzed by a single flavoproteinwas achieved via direct hydrogen transfer from a sacrificial 2-enone or 1,4-dione as hydrogen donor without requirement of a nicotinamide cofactor. Due to its simplicity, this system has clear advantages over conventional FAD-recycling systems. (C) 2009 Elsevier Ltd. All rights reserved.