Enantioselective Aminohydroxylation of Styrenyl Olefins Catalyzed by an Engineered Hemoprotein
Inha Cho
Division of Chemistry and Chemical Engineering MC 210-41, California Institute of Technology, 1200 East California Blvd, Pasadena, CA, 91125 USA
Search for more papers by this authorDr. Christopher K. Prier
Division of Chemistry and Chemical Engineering MC 210-41, California Institute of Technology, 1200 East California Blvd, Pasadena, CA, 91125 USA
Current address: Merck Research Laboratories, Merck & Co., P.O. Box 2000, Rahway, NJ, 07065 USA
Search for more papers by this authorDr. Zhi-Jun Jia
Division of Chemistry and Chemical Engineering MC 210-41, California Institute of Technology, 1200 East California Blvd, Pasadena, CA, 91125 USA
Search for more papers by this authorRuijie K. Zhang
Division of Chemistry and Chemical Engineering MC 210-41, California Institute of Technology, 1200 East California Blvd, Pasadena, CA, 91125 USA
Search for more papers by this authorDr. Tamás Görbe
Division of Chemistry and Chemical Engineering MC 210-41, California Institute of Technology, 1200 East California Blvd, Pasadena, CA, 91125 USA
Current address: School of Engineering Sciences in Chemistry, Biotechnology, and Health, KTH Royal Institute of Technology, Science for Life Laboratory 23, Tomtebodavägen, 17165 Solna, Sweden
Search for more papers by this authorCorresponding Author
Prof. Frances H. Arnold
Division of Chemistry and Chemical Engineering MC 210-41, California Institute of Technology, 1200 East California Blvd, Pasadena, CA, 91125 USA
Search for more papers by this authorInha Cho
Division of Chemistry and Chemical Engineering MC 210-41, California Institute of Technology, 1200 East California Blvd, Pasadena, CA, 91125 USA
Search for more papers by this authorDr. Christopher K. Prier
Division of Chemistry and Chemical Engineering MC 210-41, California Institute of Technology, 1200 East California Blvd, Pasadena, CA, 91125 USA
Current address: Merck Research Laboratories, Merck & Co., P.O. Box 2000, Rahway, NJ, 07065 USA
Search for more papers by this authorDr. Zhi-Jun Jia
Division of Chemistry and Chemical Engineering MC 210-41, California Institute of Technology, 1200 East California Blvd, Pasadena, CA, 91125 USA
Search for more papers by this authorRuijie K. Zhang
Division of Chemistry and Chemical Engineering MC 210-41, California Institute of Technology, 1200 East California Blvd, Pasadena, CA, 91125 USA
Search for more papers by this authorDr. Tamás Görbe
Division of Chemistry and Chemical Engineering MC 210-41, California Institute of Technology, 1200 East California Blvd, Pasadena, CA, 91125 USA
Current address: School of Engineering Sciences in Chemistry, Biotechnology, and Health, KTH Royal Institute of Technology, Science for Life Laboratory 23, Tomtebodavägen, 17165 Solna, Sweden
Search for more papers by this authorCorresponding Author
Prof. Frances H. Arnold
Division of Chemistry and Chemical Engineering MC 210-41, California Institute of Technology, 1200 East California Blvd, Pasadena, CA, 91125 USA
Search for more papers by this authorGraphical Abstract
Go direct: A hemoprotein catalyst was engineered to transform alkenes directly to amino alcohols with high enantioselectivity. Derived by directed evolution from a thermostable cytochrome c, the protein catalyst uses O-pivaloylhydroxylamine to generate a reactive iron-nitrogen species.
Abstract
Chiral 1,2-amino alcohols are widely represented in biologically active compounds from neurotransmitters to antivirals. While many synthetic methods have been developed for accessing amino alcohols, the direct aminohydroxylation of alkenes to unprotected, enantioenriched amino alcohols remains a challenge. Using directed evolution, we have engineered a hemoprotein biocatalyst based on a thermostable cytochrome c that directly transforms alkenes to amino alcohols with high enantioselectivity (up to 2500 TTN and 90 % ee) under anaerobic conditions with O-pivaloylhydroxylamine as an aminating reagent. The reaction is proposed to proceed via a reactive iron-nitrogen species generated in the enzyme active site, enabling tuning of the catalyst's activity and selectivity by protein engineering.
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