Resultats globals: 7 registres trobats en 0.01 segons.
Articles, 6 registres trobats
Documents de recerca, 1 registres trobats
Articles 6 registres trobats  
1.
12 p, 11.9 MB Getting Deeper into the Molecular Events of Heme Binding Mechanisms : A Comparative Multi-level Computational Study of HasAsm and HasAyp Hemophores / Tiessler-Sala, Laura (Universitat Autònoma de Barcelona. Departament de Química) ; Sciortino, Giuseppe (Universitat Autònoma de Barcelona. Departament de Química) ; Alonso-Cotchico, Lur (Universitat Autònoma de Barcelona. Departament de Química) ; Masgrau, Laura (Universitat Autònoma de Barcelona. Departament de Química) ; Lledós, Agustí (Universitat Autònoma de Barcelona. Departament de Química) ; Maréchal, Jean-Didier (Universitat Autònoma de Barcelona. Departament de Química)
Many biological systems obtain their activity by the inclusion of metalloporphyrins into one or several binding pockets. However, decoding the molecular mechanism under which these compounds bind to their receptors is something that has not been widely explored and is a field with open questions. [...]
2022 - 10.1021/acs.inorgchem.2c02193
Inorganic Chemistry, Vol. 61, Issue 43 (October 2022) , p. 17068-17079  
2.
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  
3.
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  
4.
12 p, 3.5 MB The effect of cofactor binding on the conformational plasticity of the biological receptors in Artificial Metalloenzymes : The case study of LmrR / Alonso-Cotchico, Lur (Universitat Autònoma de Barcelona. Departament de Química) ; Rodríguez-Guerra Pedregal, Jaime (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)
The design of Artificial Metalloenzymes (ArMs), which result from the incorporation of organometallic cofactors into biological structures, has grown steadily in the last two decades and important new-to-Nature reactions have been reached. [...]
2019 - 10.3389/fchem.2019.00211
Frontiers in chemistry, Vol. 7 (April 2019) , art. 211  
5.
36 p, 10.5 MB Defective AMH signaling disrupts GnRH neuron development and function and contributes to hypogonadotropic hypogonadism / Malone, Samuel Andrew (Jean-Pierre Aubert Research Center) ; Papadakis, Georgios E. (Lausanne University Hospital) ; Messina, Andrea (Lausanne University Hospital) ; Mimouni, Nour El Houda (Jean-Pierre Aubert Research Center) ; Trova, Sara (Jean-Pierre Aubert Research Center) ; Imbernon, Monica (Jean-Pierre Aubert Research Center) ; Allet, Cecile (Jean-Pierre Aubert Research Center) ; Cimino, Irene (Jean-Pierre Aubert Research Center) ; Acierno, James (Lausanne University Hospital) ; Cassatella, Daniele (Lausanne University Hospital) ; Xu, Cheng (Lausanne University Hospital) ; Quinton, Richard (University of Newcastle-upon-Tyne. Institute of Genetic Medicine) ; Szinnai, Gabor (University Children's Hospital Basel (Basilea, Suïssa)) ; Pigny, Pascal (Centre de Biologie Pathologie Génétique. Service Hormonologie Métabolisme Nutrition Oncologie) ; Alonso-Cotchico, Lur (Universitat Autònoma de Barcelona. Departament de Química) ; Masgrau, Laura (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Maréchal, Jean-Didier (Universitat Autònoma de Barcelona. Departament de Química) ; Prevot, V. (Jean-Pierre Aubert Research Center) ; Pitteloud, Nelly (Lausanne University Hospital) ; Giacobini, Polo (Jean-Pierre Aubert Research Center)
Congenital hypogonadotropic hypogonadism (CHH) is a condition characterized by absent puberty and infertility due to gonadotropin releasing hormone (GnRH) deficiency, which is often associated with anosmia (Kallmann syndrome, KS). [...]
2019 - 10.7554/eLife.47198
eLife, Vol. 8 (2019) , art. e47198  
6.
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  

Documents de recerca 1 registres trobats  
1.
286 p, 3.3 MB Computational design of artificial metalloenzymes / Alonso-Cotchico, Lur ; Maréchal, Jean-Didier, dir. ; Lledós, Agustí, (Lledós i Falcó) dir. ; Cairó i Badillo, Jordi Joan, dir. ; Universitat Autònoma de Barcelona. Departament de Química
El diseño enzimático es el área basada en el descubrimiento y/o optimización de biomoléculas para el desarrollo de reacciones químicas no naturales. Es un área que se encuentra en su mayor crecimiento y constituye uno de los puntos clave en la transición de la química hacia alternativas más ecológicas. [...]
Enzyme design is the scientific field that aims at discovering and/or optimizing biomolecules to reach new-to-Nature reactions. It is an area in wild expansion and constitutes one of the cornerstones of the transition of chemical practices towards greener alternatives. [...]

[Bellaterra] : Universitat Autònoma de Barcelona, 2018.  

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