Artificial Copper Enzymes for Asymmetric Diels-Alder Reactions

Peter J. Deuss, Gina Popa, Alexandra M.Z. Slawin, Wouter Laan*, Paul C.J. Kamer

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

45 Citations (Scopus)

Abstract

The development of artificial copper enzymes from sterol carrier protein type2 like domain (SCP-2L) for the use in asymmetric catalysis was explored. For this purpose, proteins were modified with various nitrogen donor ligands. Maleimide-containing ligands were found most suitable for selective cysteine bio-conjugation. Fluorescence spectroscopy was used to confirm copper binding to an introduced phenanthroline ligand, which was introduced in two unique cysteine containing SCP-2L mutants. Copper adducts of several modified SCP-2L templates were applied in asymmetric Diels-Alder reactions. A clear influence of both the protein environment and the introduced ligand was found in the asymmetric Diels-Alder reaction between azachalcone and cyclopentadiene. A promising enantioselectivity of 25% ee was obtained by using SCP-2LV83C modified with phenanthroline-maleimide ligand. Good endo selectivity was observed for SCP-2L modified with the dipicolylamine-based nitrogen donor ligand. These artificial metalloenzymes provide a suitable starting point for the implementation of various available techniques to optimise the performance of this system.

Original languageEnglish
Pages (from-to)1184-1191
Number of pages8
JournalChemCatChem
Volume5
Issue number5
DOIs
Publication statusPublished - 1 May 2013

Keywords

  • Biocatalysis
  • Copper
  • Ligand effects
  • Metalloenzymes
  • Nitrogen

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