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Enzyme- and ruthenium-catalyzed dynamic kinetic resolution involving cascade alkoxycarbonylations for asymmetric synthesis of 5-Substituted N-Aryloxazolidinones
KTH Royal Instute of Technology, Sweden.
KTH Royal Instute of Technology, Sweden.
KTH Royal Instute of Technology, Sweden;Univ Massachusetts Lowell, USA.
Linnaeus University, Faculty of Health and Life Sciences, Department of Chemistry and Biomedical Sciences. KTH Royal Instute of Technology, Sweden;Univ Massachusetts Lowell, USA. (Lnuc BMC;BBCL)ORCID iD: 0000-0002-1533-6514
2019 (English)In: Molecular Catalysis, ISSN 2468-8274, Vol. 470, p. 138-144Article in journal (Refereed) Published
Abstract [en]

Asymmetric synthesis of N-aryloxazolidinones via dynamic kinetic resolution was developed. A ruthenium-based catalyst was used in the racemization of β-anilino alcohols, while Candida antarctica lipase B (CAL-B) was applied for two selective alkoxycarbonylations operating in cascade. Various N-aryloxazolidinone derivatives were obtained in high yields and good enantiopurities. © 2019 Elsevier B.V.

Place, publisher, year, edition, pages
Elsevier, 2019. Vol. 470, p. 138-144
Keywords [en]
Asymmetric synthesis, Candida Antarctica lipase B, Cascade alkoxycarbonylation, Dynamic kinetic resolution, Oxazolidinone, Candida, Isomers, Ruthenium, Yeast, Alkoxycarbonylation, Oxazolidinones, Kinetics
National Category
Biochemistry Molecular Biology
Research subject
Chemistry, Biochemistry
Identifiers
URN: urn:nbn:se:lnu:diva-82851DOI: 10.1016/j.mcat.2019.03.020ISI: 000469906600017Scopus ID: 2-s2.0-85063965626OAI: oai:DiVA.org:lnu-82851DiVA, id: diva2:1317553
Available from: 2019-05-23 Created: 2019-05-23 Last updated: 2025-09-23Bibliographically approved

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Ramström, Olof

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CiteExportLink to record
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