4.3 Review

Artificial Metalloenzymes for Asymmetric Catalysis by Creation of Novel Active Sites in Protein and DNA Scaffolds

Journal

ISRAEL JOURNAL OF CHEMISTRY
Volume 55, Issue 1, Pages 21-31

Publisher

WILEY-V C H VERLAG GMBH
DOI: 10.1002/ijch.201400094

Keywords

asymmetric catalysis; biocatalysis; DNA; metalloenzymes; metalloproteins

Funding

  1. Netherlands Research School Combination Catalysis (NRSC-C)
  2. Netherlands Organization for Scientific Research (NWO)
  3. University of Groningen
  4. European Research Council (ERC) [280010]
  5. Ministry of Education Culture and Science of the Netherlands [024.001.035]
  6. European Research Council (ERC) [280010] Funding Source: European Research Council (ERC)

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Artificial metalloenzymes have emerged as a promising new approach to asymmetric catalysis. In our group, we are exploring novel artificial metalloenzyme designs involving creation of a new active site in a protein or DNA scaffold that does not have an existing binding pocket. In this review, we give an overview of the developments in the two approaches to artificial metalloenzymes for asymmetric catalysis investigated in our group: creation of a novel active site on a peptide or protein dimer interface and using DNA as a scaffold for artificial metalloenzymes.

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