Artificial Metalloenzymes for Enantioselective Catalysis Based on the Noncovalent Incorporation of Organometallic Moieties in a Host Protein
JournalArticle (Originalarbeit in einer wissenschaftlichen Zeitschrift)
 
ID 116782
Author(s) Ward, Thomas R.
Author(s) at UniBasel Ward, Thomas R.
Year 2005
Title Artificial Metalloenzymes for Enantioselective Catalysis Based on the Noncovalent Incorporation of Organometallic Moieties in a Host Protein
Journal Chemistry - A European Journal
Volume 11
Number 13
Pages / Article-Number 3798-804
Keywords artificial metalloenzymes, asymmetric catalysis, biotin-avidin technology, chemogenetic optimization, hydrogenation
Abstract Enzymatic and homogeneous catalysis offer complementary means to produce enantiopure products. Incorporation of achiral, biotinylated aminodiphosphine–rhodium complexes in (strept)avidin affords enantioselective hydrogenation catalysts. A combined chemogenetic procedure allows the optimization of the activity and the selectivity of such artificial metalloenzymes: the reduction of acetamidoacrylate proceeds to produce N-acetamidoalanine in either 96 % ee (R) or 80 % ee (S). In addition to providing a chiral second coordination sphere and, thus, selectivity to the catalyst, the phenomenon of protein-accelerated catalysis (e.g., increased activity) was unraveled. Such artificial metalloenzymes based on the biotin–avidin technology display features that are reminiscent of both homogeneous and of enzymatic catalysis.
Publisher Wiley
ISSN/ISBN 0947-6539 ; 1521-3765
edoc-URL http://edoc.unibas.ch/dok/A5254497
Full Text on edoc No
Digital Object Identifier DOI 10.1002/chem.200401232
PubMed ID http://www.ncbi.nlm.nih.gov/pubmed/15761912
ISI-Number WOS:000230071100002
Document type (ISI) Journal Article
 
   

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