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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. (Linnaeus Ctr Biomat Chem, 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 and 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: 2022-03-15Bibliographically approved

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Ramström, Olof

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