ArticleChembiochem : a European journal of chemical biology2021
An Artificial Cofactor Catalyzing the Baylis-Hillman Reaction with Designed Streptavidin as Protein Host*.
Article in Chembiochem : a European journal of chemical biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Article
- Recent progress and prospects in the organocatalytic Morita-Baylis-Hillman reaction.RSC advances · 2024Review
- An artificial nickel chlorinase based on the biotin-streptavidin technology.Chemical communications (Cambridge, England) · 2024Article
- Artificial Metalloenzyme-Catalyzed Enantioselective Amidation via Nitrene Insertion in Unactivated C(Journal of the American Chemical Society · 2023Article
- Derivatives of Natural Organocatalytic Cofactors and Artificial Organocatalytic Cofactors as Catalysts in Enzymes.Chembiochem : a European journal of chemical biology · 2022Review
- The role of streptavidin and its variants in catalysis by biotinylated secondary amines.Organic & biomolecular chemistry · 2021Article
- An Artificial Cofactor Catalyzing the Baylis-Hillman Reaction with Designed Streptavidin as Protein Host*.Chembiochem : a European journal of chemical biology · 2021Article
- Transfer hydrogenations catalyzed by streptavidin-hosted secondary amine organocatalysts.Chemical communications (Cambridge, England) · 2021Article
- Streptavidin-Hosted Organocatalytic Aldol Addition.Molecules (Basel, Switzerland) · 2020Article
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Authors and funding
4 authors.
Funding
Abstract
An artificial cofactor based on an organocatalyst embedded in a protein has been used to conduct the Baylis-Hillman reaction in a buffered system. As protein host, we chose streptavidin, as it can be easily crystallized and thereby supports the design process. The protein host around the cofactor was rationally designed on the basis of high-resolution crystal structures obtained after each variation of the amino acid sequence. Additionally, DFT-calculated intermediates and transition states were used to rationalize the observed activity. Finally, repeated cycles of structure determination and redesign led to a system with an up to one order of magnitude increase in activity over the bare cofactor and to the most active proteinogenic catalyst for the Baylis-Hillman reaction known today.
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