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Chemoenzymatic Deracemization of Chiral Sulfoxides

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F18%3A10378060" target="_blank" >RIV/00216208:11310/18:10378060 - isvavai.cz</a>

  • Result on the web

    <a href="https://doi.org/10.1002/anie.201805858" target="_blank" >https://doi.org/10.1002/anie.201805858</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1002/anie.201805858" target="_blank" >10.1002/anie.201805858</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Chemoenzymatic Deracemization of Chiral Sulfoxides

  • Original language description

    The highly enantioselective enzyme methionine sulfoxide reductaseA was combined with an oxaziridine-type oxidant in a biphasic setup for the deracemization of chiral sulfoxides. Remarkably, high eevalues were observed with a wide range of substrates, thus providing a practical route for the synthesis of enantiomerically pure sulfoxides.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10401 - Organic chemistry

Result continuities

  • Project

    <a href="/en/project/GJ17-25897Y" target="_blank" >GJ17-25897Y: Development of Fluorescent Probes for Methionine Sulfoxide Reductase and Beyond</a><br>

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Others

  • Publication year

    2018

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Angewandte Chemie - International Edition

  • ISSN

    1433-7851

  • e-ISSN

  • Volume of the periodical

    57

  • Issue of the periodical within the volume

    31

  • Country of publishing house

    DE - GERMANY

  • Number of pages

    4

  • Pages from-to

    9849-9852

  • UT code for WoS article

    000439741900047

  • EID of the result in the Scopus database

    2-s2.0-85050488808