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Peer-reviewedCC BY 4.0Chemistry - A European Journal

Covalent Insertion of a Mn(Salen) Type Complex in Cross-Linked Protein Crystals: Design of an Enantioselective Artificial Epoxidase

  • Manel Boukhallat
  • Ismail Benhamed
  • Jade Arnone
  • Stann van Barren
  • Clara Rinaldi
  • Patrice Catty
  • Caroline Marchi- Delapierre
  • Christine Cavazza
  • Stéphane Ménage
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Abstract

Artificial enzymes represent a promising alternative for performing non-natural reactions in biocatalysis. Here, we illustrate the potential of cross-linked enzyme crystals (CLEC) to achieve enantioselective epoxidation through the generation of an artificial enzyme obtained by direct covalent anchoring of a manganese complex as an artificial active site within a protein. Enantiomeric excess (ee) of up to 90% on cis-beta-methylstyrene was measured when the covalent binding yield was maximized, thanks to the remarkable behavior of the crystals. The structure of the modified enzyme, NikA, is provided. This work adds to the growing body of examples highlighting the advantages of CLEC in oxidation catalysis.

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Cite

BibTeXRIS
BibTeX
@article{boukhallat2026covalent,
  title = {{Covalent Insertion of a Mn(Salen) Type Complex in Cross-Linked Protein Crystals: Design of an Enantioselective Artificial Epoxidase}},
  author = {Manel Boukhallat and Ismail Benhamed and Jade Arnone and Stann van Barren and Clara Rinaldi and Patrice Catty and Caroline Marchi- Delapierre and Christine Cavazza and Stéphane Ménage},
  journal = {Chemistry - A European Journal},
  year = {2026},
  month = oct,
  doi = {10.1002/chem.71159},
  url = {https://hal.science/hal-05659284v1},
  note = {CC BY 4.0},
}
RIS
TY  - JOUR
TI  - Covalent Insertion of a Mn(Salen) Type Complex in Cross-Linked Protein Crystals: Design of an Enantioselective Artificial Epoxidase
AU  - Manel Boukhallat
AU  - Ismail Benhamed
AU  - Jade Arnone
AU  - Stann van Barren
AU  - Clara Rinaldi
AU  - Patrice Catty
AU  - Caroline Marchi- Delapierre
AU  - Christine Cavazza
AU  - Stéphane Ménage
PY  - 2026
DA  - 2026/10/07
JO  - Chemistry - A European Journal
DO  - 10.1002/chem.71159
UR  - https://hal.science/hal-05659284v1
AB  - Artificial enzymes represent a promising alternative for performing non-natural reactions in biocatalysis. Here, we illustrate the potential of cross-linked enzyme crystals (CLEC) to achieve enantioselective epoxidation through the generation of an artificial enzyme obtained by direct covalent anchoring of a manganese complex as an artificial active site within a protein. Enantiomeric excess (ee) of up to 90% on cis-beta-methylstyrene was measured when the covalent binding yield was maximized, thanks to the remarkable behavior of the crystals. The structure of the modified enzyme, NikA, is provided. This work adds to the growing body of examples highlighting the advantages of CLEC in oxidation catalysis.
SN  - 0947-6539
SN  - 1521-3765
ER  -