Nicotinamide-independent asymmetric bioreduction of C[bond, double bond]C-bonds via disproportionation of enones catalyzed by enoate reductases

The asymmetric bioreduction of activated C[bond, double bond]C-bonds catalyzed by a single flavoprotein was 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 adv...

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Detalles Bibliográficos
Autores principales: Stueckler, Clemens, Reiter, Tamara C., Baudendistel, Nina, Faber, Kurt
Formato: Texto
Lenguaje:English
Publicado: Pergamon Press 2010
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3007678/
https://www.ncbi.nlm.nih.gov/pubmed/21270958
http://dx.doi.org/10.1016/j.tet.2009.11.065
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author Stueckler, Clemens
Reiter, Tamara C.
Baudendistel, Nina
Faber, Kurt
author_facet Stueckler, Clemens
Reiter, Tamara C.
Baudendistel, Nina
Faber, Kurt
author_sort Stueckler, Clemens
collection PubMed
description The asymmetric bioreduction of activated C[bond, double bond]C-bonds catalyzed by a single flavoprotein was 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.
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spelling pubmed-30076782011-01-24 Nicotinamide-independent asymmetric bioreduction of C[bond, double bond]C-bonds via disproportionation of enones catalyzed by enoate reductases Stueckler, Clemens Reiter, Tamara C. Baudendistel, Nina Faber, Kurt Tetrahedron Article The asymmetric bioreduction of activated C[bond, double bond]C-bonds catalyzed by a single flavoprotein was 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. Pergamon Press 2010-01-16 /pmc/articles/PMC3007678/ /pubmed/21270958 http://dx.doi.org/10.1016/j.tet.2009.11.065 Text en © 2010 Elsevier Ltd. https://creativecommons.org/licenses/by-nc-nd/3.0/Open Access under CC BY-NC-ND 3.0 (https://creativecommons.org/licenses/by-nc-nd/3.0/) license
spellingShingle Article
Stueckler, Clemens
Reiter, Tamara C.
Baudendistel, Nina
Faber, Kurt
Nicotinamide-independent asymmetric bioreduction of C[bond, double bond]C-bonds via disproportionation of enones catalyzed by enoate reductases
title Nicotinamide-independent asymmetric bioreduction of C[bond, double bond]C-bonds via disproportionation of enones catalyzed by enoate reductases
title_full Nicotinamide-independent asymmetric bioreduction of C[bond, double bond]C-bonds via disproportionation of enones catalyzed by enoate reductases
title_fullStr Nicotinamide-independent asymmetric bioreduction of C[bond, double bond]C-bonds via disproportionation of enones catalyzed by enoate reductases
title_full_unstemmed Nicotinamide-independent asymmetric bioreduction of C[bond, double bond]C-bonds via disproportionation of enones catalyzed by enoate reductases
title_short Nicotinamide-independent asymmetric bioreduction of C[bond, double bond]C-bonds via disproportionation of enones catalyzed by enoate reductases
title_sort nicotinamide-independent asymmetric bioreduction of c[bond, double bond]c-bonds via disproportionation of enones catalyzed by enoate reductases
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3007678/
https://www.ncbi.nlm.nih.gov/pubmed/21270958
http://dx.doi.org/10.1016/j.tet.2009.11.065
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