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Asymmetric Reductive Carbocyclization Using Engineered Ene Reductases.

Kathrin Heckenbichler¹, Anna Schweiger¹, Lea Alexandra Brandner¹

¹Institute of Organic Chemistry, Graz University of Technology, Stremayrgasse 9, 8010, Graz, Austria.

Angewandte Chemie (International Ed. in English)

|April 25, 2018

Summary

Old Yellow Enzyme (OYE) family enzymes catalyze novel C-C bond formation via reductive cyclization. This discovery expands their biocatalytic applications, enabling enantioselective synthesis of chiral cyclopropanes with high purity.

Keywords:

C−C-bond formation asymmetric synthesis biocatalysis enoate reductases protein engineering

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Area of Science:

Biocatalysis
Enzyme Engineering
Organic Chemistry

Background:

Old Yellow Enzyme (OYE) family enzymes are known for asymmetric reduction of C=C bonds in electron-deficient α,β-unsaturated compounds.
This canonical function has been widely applied in biocatalysis for stereoselective synthesis.

Purpose of the Study:

To explore novel catalytic activities of OYE family enzymes beyond their known reduction function.
To investigate the potential of OYE enzymes in catalyzing C-C bond formation reactions.
To develop a new biocatalytic method for enantioselective synthesis of cyclic compounds.

Main Methods:

Investigated the reactivity of OYE enzymes with α,β-unsaturated aldehydes and ketones possessing an additional electrophilic group.
Employed site-directed mutagenesis, specifically replacing a key tyrosine residue with phenylalanine or tryptophan.
Analyzed reaction products using chiral chromatography to determine enantiomeric excess (ee).

Main Results:

Demonstrated that OYE enzymes can catalyze reductive cyclization, forming C-C bonds.
Mutating a crucial tyrosine residue to phenylalanine or tryptophan shifted enzyme activity towards cyclization over reduction.
Achieved highly enantioselective synthesis of chiral cyclopropanes, with enantiomeric excess exceeding 99%.

Conclusions:

OYE enzymes exhibit a previously unrecognized capability for catalyzing C-C bond formation through reductive cyclization.
Enzyme engineering by single-site mutation can redirect OYE activity towards cyclization.
This work presents a novel biocatalytic route for the efficient and enantioselective synthesis of valuable chiral cyclopropane structures.