2014
DOI: 10.1002/ijch.201400094
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Artificial Metalloenzymes for Asymmetric Catalysis by Creation of Novel Active Sites in Protein and DNA Scaffolds

Abstract: 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 us… Show more

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Cited by 23 publications
(13 citation statements)
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“…Over the years, different approaches have been explored to develop such artificial enzymes, and these methods have been widely reviewed [17][18][19][20][21][22][23][24][25][26]. As a consequence, we will only summarize the most prominent and latest results in the following (sections 2.1 to 2.4).…”
Section: The Artificial Metalloenzyme Approachmentioning
confidence: 97%
“…Over the years, different approaches have been explored to develop such artificial enzymes, and these methods have been widely reviewed [17][18][19][20][21][22][23][24][25][26]. As a consequence, we will only summarize the most prominent and latest results in the following (sections 2.1 to 2.4).…”
Section: The Artificial Metalloenzyme Approachmentioning
confidence: 97%
“…[2][3][4][5][6] A popular approach to achieve enzymatic catalysis of reactions that have no equivalent in nature involves the creation of artificial metalloenzymes, which are rationally designed hybrids of proteins with abiological catalytically active metal cofactors. [7][8][9][10][11][12][13] In this approach, the basal catalytic activity is supplied by the metal complex, whereas the second coordination sphere interactions provided by the protein scaffold are envisioned to contribute to rate acceleration and (enantio-)selectivity. Since the protein scaffolds used have not naturally evolved for the reaction of interest, usually the active site structure is far from optimal.…”
Section: Main Textmentioning
confidence: 99%
“…The one-handed double-helical structure has the potential to be a promising chiral framework for enantioselective catalysis and template-directed asymmetric synthesis as exemplified by the DNA-based hybrid biocatalysts [1] and DNA-templated stereoselective reactions. [2] Although the helicates [3] and aromatic oligoamides [4] are well-established to form double helices through self-assembly driven by metal coordination and hydrogen bonding/aromatic stacking interactions, respectively, their application to supramolecular asymmetric catalysis and template-directed asymmetric synthesis has been rather limited.…”
Section: Introductionmentioning
confidence: 99%