Browsing by Author "Lucas, Fátima"
Now showing items 1-6 of 6
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Asymmetric sulfoxidation by engineering the heme pocket of a dye-decolorizing peroxidase
Linde, Dolores; Cañellas, Marina; Coscolín, Cristina; Davó-Siguero, Irene; Romero, Antonio; Lucas, Fátima; Ruiz-Dueñas, Francisco J.; Guallar, Víctor; Martínez, Ángel T. (Royal Society of Chemistry, 2016-05-23)
Article
Open AccessThe so-called dye-decolorizing peroxidases (DyPs) constitute a new family of proteins exhibiting remarkable stability. With the aim of providing them new catalytic activities of biotechnological interest, the heme pocket ... -
Catalytic surface radical in dye-decolorizing peroxidase: A computational, spectroscopic and directed mutagenesis study
Linde, Dolores; Pogni, Rebecca; Cañellas, Marina; Lucas, Fátima; Guallar, Víctor; Ruiz-Dueñas, Francisco J.; Baratto, Maria Camilla; Sinocro, Adalgisa; Coscolin, Cristina; Romero, Antonio; Medrano, Francisco Javier; Martínez, Angel T. (Portland Press, 2015-03-01)
Article
Open AccessDye-decolorizing peroxidase (DyP) of Auricularia auriculajudae has been expressed in Escherichia coli as a representative of a new DyP family, and subjected to mutagenic, spectroscopic, crystallographic and computational ... -
Molecular determinants for selective C 25-hydroxylation of vitamins D 2 and D 3 by fungal peroxygenases
Lucas, Fátima; Babot, Esteban D.; Cañellas, Marina; del Río, José C.; Kalum, Lisbeth; Ullrich, René; Hofrichter, Martin; Guallar, Víctor; Martínez, Ángel T.; Gutiérrez, Ana (Royal Society of Chemistry, 2015-08-07)
Article
Open AccessHydroxylation of vitamin D by Agrocybe aegerita and Coprinopsis cinerea peroxygenases was investigated in a combined experimental and computational study. 25-Monohydroxylated vitamin D3 (cholecalciferol) and D2 (ergocalciferol), ... -
Molecular Modeling in Enzyme Design, Toward In Silico Guided Directed Evolution
Monza, Emanuele; Acebes, Sandra; Lucas, Fátima; Guallar, Victor (Springer, 2017-02-15)
Part of book or chapter of book
Open AccessDirected evolution (DE) creates diversity in subsequent rounds of mutagenesis in the quest of increased protein stability, substrate binding, and catalysis. Although this technique does not require any structural/mechanistic ... -
Oxidoreductases on their way to industrial biotransformations
Martinez, Angel T.; Ruiz-Dueñas, Francisco; Camarero, Susana; Serrano, Ana; Linde, Dolores; Lund, Henrik; Vind, Jesper; Tovborg, Morten; Herold-Majumdar, Owik M.; Hofrichter, Martin; Liers, Christiane; Ullrich, René; Scheibner, Katrin; Sannia, Giovanni; Piscitelli, Alessandra; Pezzella, Cinzia; Sener, Mehmet E.; Kiliç, Sibel; van Berkel, Willhem J.H.; Guallar, Victor; Lucas, Fátima; Zuhse, Ralf; Ludwig, Roland; Hollmann, Frank; Fernández-Fueyo, Elena; Record, Eric; Faulds, Craig B.; Tortajada, Marta; Winckelmann, Ib; Rasmussen, Jo-Anne; Gelo-Pujic, Mirjana; Gutiérrez, Ana; del Río, José C.; Rencoret, Jorge; Alcalde, Miguel (Elsevier, 2017-11)
Article
Open AccessFungi produce heme-containing peroxidases and peroxygenases, flavin-containing oxidases and dehydrogenases, and different copper-containing oxidoreductases involved in the biodegradation of lignin and other recalcitrant ... -
Re-designing the substrate binding pocket of laccase for enhanced oxidation of sinapic acid
Pardo, Isabel; Santiago, Gerard; Gentili, Patrizia; Lucas, Fátima; Monza, Emanuele; Medrano, Francisco Javier; Galli, Carlo; Martínez, Angel T.; Guallar, Víctor; Camarero, Susana (Royal Society of Chemistry, 2015-12-29)
Article
Open AccessIterative saturation mutagenesis was performed over six residues delimiting the substrate binding pocket of a high redox potential chimeric laccase with the aim of enhancing its activity over sinapic acid, a ligninrelated ...