A Dual Anchoring Strategy for the Localization and Activation of Artificial Metalloenzymes Based on the Biotin-Streptavidin Technology
JournalArticle (Originalarbeit in einer wissenschaftlichen Zeitschrift)
 
ID 1878418
Author(s) Zimbron, Jeremy M.; Heinisch, Tillmann; Schmid, Maurus; Hamels, Didier; Nogueira, Elisa S.; Schirmer, Tilman; Ward, Thomas R.
Author(s) at UniBasel Schirmer, Tilman
Ward, Thomas R.
Nogueira, Elisa
Year 2013
Year: comment 2013
Title A Dual Anchoring Strategy for the Localization and Activation of Artificial Metalloenzymes Based on the Biotin-Streptavidin Technology
Journal Journal of the American Chemical Society
Volume 135
Number 14
Pages / Article-Number 5384-5388
Abstract Artificial metalloenzymes result from anchoring an active catalyst within a protein environment. Toward this goal, various localization strategies have been pursued: covalent, supramolecular, or dative anchoring. Herein we show that introduction of a suitably positioned histidine residue contributes to firmly anchor, via a dative bond, a biotinylated rhodium piano stool complex within streptavidin. The in silico design of the artificial metalloenzyme was confirmed by X-ray crystallography. The resulting artificial metalloenzyme displays significantly improved catalytic performance, both in terms of activity and selectivity in the transfer hydrogenation of imines. Depending on the position of the histidine residue, both enantiomers of the salsolidine product can be obtained.
Publisher American Chemical Society
ISSN/ISBN 0002-7863 ; 1520-5126
edoc-URL http://edoc.unibas.ch/dok/A6146150
Full Text on edoc Available
Digital Object Identifier DOI 10.1021/ja309974s
PubMed ID http://www.ncbi.nlm.nih.gov/pubmed/23496309
ISI-Number 000317548400039
Document type (ISI) Article
 
   

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