An enantioselective artificial Suzukiase based on the biotin–streptavidin technology

Introduction of a biotinylated monophosphine palladium complex within streptavidin affords an enantioselective artificial Suzukiase. Site-directed mutagenesis allowed the optimization of the activity and the enantioselectivity of this artificial metalloenzyme. A variety of atropisomeric biaryls were...

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Autores principales: Chatterjee, Anamitra, Mallin, Hendrik, Klehr, Juliane, Vallapurackal, Jaicy, Finke, Aaron D., Vera, Laura, Marsh, May, Ward, Thomas R.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Royal Society of Chemistry 2016
Materias:
Chemistry
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5953008/
https://www.ncbi.nlm.nih.gov/pubmed/29896353
http://dx.doi.org/10.1039/c5sc03116h
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author Chatterjee, Anamitra
Mallin, Hendrik
Klehr, Juliane
Vallapurackal, Jaicy
Finke, Aaron D.
Vera, Laura
Marsh, May
Ward, Thomas R.
author_facet Chatterjee, Anamitra
Mallin, Hendrik
Klehr, Juliane
Vallapurackal, Jaicy
Finke, Aaron D.
Vera, Laura
Marsh, May
Ward, Thomas R.
author_sort Chatterjee, Anamitra
collection PubMed
description Introduction of a biotinylated monophosphine palladium complex within streptavidin affords an enantioselective artificial Suzukiase. Site-directed mutagenesis allowed the optimization of the activity and the enantioselectivity of this artificial metalloenzyme. A variety of atropisomeric biaryls were produced in good yields and up to 90% ee. The hybrid catalyst described herein shows comparable TOF to the previous aqueous-asymmetric Suzuki catalysts, and excellent stability under the reaction conditions to realize higher TON through longer reaction time.
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spelling pubmed-59530082018-06-12 An enantioselective artificial Suzukiase based on the biotin–streptavidin technology Chatterjee, Anamitra Mallin, Hendrik Klehr, Juliane Vallapurackal, Jaicy Finke, Aaron D. Vera, Laura Marsh, May Ward, Thomas R. Chem Sci Chemistry Introduction of a biotinylated monophosphine palladium complex within streptavidin affords an enantioselective artificial Suzukiase. Site-directed mutagenesis allowed the optimization of the activity and the enantioselectivity of this artificial metalloenzyme. A variety of atropisomeric biaryls were produced in good yields and up to 90% ee. The hybrid catalyst described herein shows comparable TOF to the previous aqueous-asymmetric Suzuki catalysts, and excellent stability under the reaction conditions to realize higher TON through longer reaction time. Royal Society of Chemistry 2016-01-01 2015-10-19 /pmc/articles/PMC5953008/ /pubmed/29896353 http://dx.doi.org/10.1039/c5sc03116h Text en This journal is © The Royal Society of Chemistry 2016 http://creativecommons.org/licenses/by/3.0/ This article is freely available. This article is licensed under a Creative Commons Attribution 3.0 Unported Licence (CC BY 3.0)
spellingShingle Chemistry
Chatterjee, Anamitra
Mallin, Hendrik
Klehr, Juliane
Vallapurackal, Jaicy
Finke, Aaron D.
Vera, Laura
Marsh, May
Ward, Thomas R.
An enantioselective artificial Suzukiase based on the biotin–streptavidin technology
title An enantioselective artificial Suzukiase based on the biotin–streptavidin technology
title_full An enantioselective artificial Suzukiase based on the biotin–streptavidin technology
title_fullStr An enantioselective artificial Suzukiase based on the biotin–streptavidin technology
title_full_unstemmed An enantioselective artificial Suzukiase based on the biotin–streptavidin technology
title_short An enantioselective artificial Suzukiase based on the biotin–streptavidin technology
title_sort enantioselective artificial suzukiase based on the biotin–streptavidin technology
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5953008/
https://www.ncbi.nlm.nih.gov/pubmed/29896353
http://dx.doi.org/10.1039/c5sc03116h
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