Bypassing Biocatalytic Substrate Limitations in Oxidative Dearomatization Reactions by Transient Substrate Mimicking

Enzymatic oxidative dearomatization is an efficient way to generate chiral molecules from simple arenes. One example is the flavin-dependent monooxygenase SorbC involved in sorbicillinoid biosynthesis. However, SorbC requires a long-chain keto substituent at its phenolic substrate, thus preventing i...

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Published inOrganic letters Vol. 21; no. 12; pp. 4520 - 4524
Main Authors Milzarek, Tobias M, Einsiedler, Manuel, Aldemir, Hülya, D’Agostino, Paul M, Evers, Julia K, Hertrampf, Gesa, Lamm, Katharina, Malay, Mert, Matura, Anke, Müller, Jonas I, Gulder, Tobias A. M
Format Journal Article
LanguageEnglish
Published WASHINGTON American Chemical Society 21.06.2019
Amer Chemical Soc
Subjects
Chemistry
Chemistry, Organic
Physical Sciences
Science & Technology
AROMATIC-HYDROCARBONS
MICROORGANISMS
DEGRADATION
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Summary:Enzymatic oxidative dearomatization is an efficient way to generate chiral molecules from simple arenes. One example is the flavin-dependent monooxygenase SorbC involved in sorbicillinoid biosynthesis. However, SorbC requires a long-chain keto substituent at its phenolic substrate, thus preventing its application beyond the synthesis of natural sorbicillinoids or close structural analogues. This work describes an approach to broaden the accessible product spectrum of SorbC by employing an ester functionality mimicking the natural substrate structure during enzymatic oxidation.
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ISSN:1523-7060
1523-7052
DOI:10.1021/acs.orglett.9b01398