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

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 giv...

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Bibliographic Details
Published inIsrael journal of chemistry Vol. 55; no. 1; pp. 21 - 31
Main Authors Drienovská, Ivana, Roelfes, Gerard
Format Journal Article
LanguageEnglish
Published Weinheim WILEY-VCH Verlag 01.01.2015
WILEY‐VCH Verlag
Wiley Subscription Services, Inc
Subjects
asymmetric catalysis
Asymmetry
Binding
biocatalysis
Catalysis
Crystal structure
Deoxyribonucleic acid
Dimers
DNA
metalloenzymes
metalloproteins
Pocket
Proteins
Scaffolds
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Summary: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.
Bibliography:European Research Council - No. 280010
Netherlands Organization for Scientific Research (NWO)
University of Groningen
Ministry of Education Culture and Science of the Netherlands - No. 024.001.035
Netherlands Research School Combination Catalysis (NRSC-C)
ark:/67375/WNG-9V91LGNK-0
ArticleID:IJCH201400094
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ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0021-2148
1869-5868
DOI:10.1002/ijch.201400094