Resultats globals: 3 registres trobats en 0.02 segons.
Articles, 3 registres trobats
Articles 3 registres trobats  
1.
8 p, 4.1 MB Cofactor Binding Dynamics Influence the Catalytic Activity and Selectivity of an Artificial Metalloenzyme / Villarino, Lara (University of Groningen) ; Chordia, Shreyans (University of Groningen) ; Alonso-Cotchico, Lur (University of Groningen) ; Reddem, Eswar (University of Groningen) ; Zhou, Zhi (University of Groningen) ; Thunnissen, Andy Mark W. H. (University of Groningen) ; Maréchal, Jean-Didier (Universitat Autònoma de Barcelona. Departament de Química) ; Roelfes, Gerard (University of Groningen)
We present an artificial metalloenzyme based on the transcriptional regulator LmrR that exhibits dynamics involving the positioning of its abiological metal cofactor. The position of the cofactor, in turn, was found to be related to the preferred catalytic reactivity, which is either the enantioselective Friedel-Crafts alkylation of indoles with β-substituted enones or the tandem Friedel-Crafts alkylation/enantioselective protonation of indoles with α-substituted enones. [...]
2020 - 10.1021/acscatal.0c01619
ACS catalysis, Vol. 10, Num 20 (2020) , p. 11783-11790  
2.
5 p, 2.2 MB An Artificial Heme Enzyme for Cyclopropanation Reactions / Villarino, Lara (University of Groningen. Stratingh Institute for Chemistry) ; Splan, Kathryn E. (Macalester College. Department of Chemistry) ; Reddem, Eswar (University of Groningen. Stratingh Institute for Chemistry) ; Alonso-Cotchico, Lur (Universitat Autònoma de Barcelona. Departament de Química) ; Gutiérrez de Souza, Cora (University of Groningen. Stratingh Institute for Chemistry) ; Lledós, Agustí (Lledós i Falcó) (Universitat Autònoma de Barcelona. Departament de Química) ; Maréchal, Jean-Didier (Universitat Autònoma de Barcelona. Departament de Química) ; Thunnissen, Andy-Mark W. H. (University of Groningen. Stratingh Institute for Chemistry) ; Roelfes, Gerard (University of Groningen. Stratingh Institute for Chemistry)
An artificial heme enzyme was created through self-assembly from hemin and the lactococcal multidrug resistance regulator (LmrR). The crystal structure shows the heme bound inside the hydrophobic pore of the protein, where it appears inaccessible for substrates. [...]
2018 - 10.1002/anie.201802946
Angewandte Chemie (International ed. Internet), Vol. 57, Issue 26 (June 2018) , p. 7785-7789  
3.
8 p, 830.0 KB Design of an enantioselective artificial metallo-hydratase enzyme containing an unnatural metal-binding amino acid / Drienovská, Ivana (Stratingh Institute for Chemistry) ; Alonso-Cotchico, Lur (Universitat Autònoma de Barcelona. Departament de Química) ; Vidossich, Pietro (Universitat Autònoma de Barcelona. Departament de Química) ; Lledós, Agustí (Lledós i Falcó) (Universitat Autònoma de Barcelona. Departament de Química) ; Maréchal, Jean-Didier (Universitat Autònoma de Barcelona. Departament de Química) ; Roelfes, Gerard (Stratingh Institute for Chemistry)
Starting from biochemical knowledge followed by computational design, an artificial metallo-hydratase comprising an unnatural metal binding amino acid was created. The design of artificial metalloenzymes is a challenging, yet ultimately highly rewarding objective because of the potential for accessing new-to-nature reactions. [...]
2017 - 10.1039/c7sc03477f
Chemical science, Vol. 8 (Oct. 2017) , p. 7228-7235  

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