Optimized oxidoreductases for medium and large scale industrial biotransformations
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Project Secretariat
Dr Marta Pérez-Boada
E-mail: MPBoada@cib.csic.es
Consejo Superior de Investigaciones Científicas (CSIC)
Biological Research Centre (CIB)
Calle Ramiro de Maeztu 9, E-28040 Madrid, Spain
Phone: 34 918373112
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publications
Total records: 112
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[ 2016 ] Linde D, Cañellas M, Coscolín C, Davó-Siguero I, Romero A, Lucas F, Ruiz-Dueñas FJ, Guallar V, Martínez AT Asymmetric sulfoxidation by engineering the heme pocket of a dye-decolorizing peroxidase: An experimental and computational study Catal. Sci. Technol., 6: 6277-6285
[ 2016 ] Lourenço A, Rencoret J, Chemetova C, Gominho J, Gutiérrez A, del Río JC, Pereira H Lignin Composition and Structure Differs between Xylem, Phloem and Phellem in Quercus suber L. Front. Plant Sci., 7: 1612
[ 2016 ] Lucas F, Babot ED, Cañellas M, del Río JC, Kalum L, Ullrich R, Hofrichter M, Guallar V, Martínez AT, Gutiérrez A Molecular determinants for selective C25-hydroxylation of vitamins D2 and D3 by fungal peroxygenases Catal. Sci. Technol., 6: 288-295
[ 2016 ] Martínez AT How to break down crystalline cellulose Science, 352: 1050-1051
[ 2016 ] Maté D, Alcalde M Laccase: a multi-purpose biocatalyst at the forefront of biotechnology Microbial Biotechnol., doi: 10.1111/1751-7915.12422
[ 2016 ] Mathieu Y, Piumi F, Valli R, Carro J, Ferreira P, Faulds CB, Record E Activities of Secreted Aryl Alcohol Quinone Oxidoreductases from Pycnoporus cinnabarinus Provide Insights into Fungal Degradation of Plant Biomass Appl. Environ. Microbiol., 82: 2411-2423
year2017
Mapping the Long-Range Electron Transfer Route in Ligninolytic Peroxidases
Acebes S, Ruiz-Dueñas FJ, Toubes M, Saez-Jimenez V, Pérez-Boada M, Lucas F, Martínez AT, Guallar V
J. Phys. Chem. B, 121: 3946-3954

Combining a computational analysis with site-directed mutagenesis, we have studied the long-range electron transfer pathway in versatile and lignin peroxidases, two enzymes of biotechnological interest that play a key role for fungal degradation of the bulky lignin molecule in plant biomass. The in silico study established two possible electron transfer routes starting at the surface tryptophan residue previously identified as responsible for oxidation of the bulky lignin polymer. Moreover, in both enzymes, a second buried tryptophan residue appears as a top electron transfer carrier, indicating the prevalence of one pathway. Site-directed mutagenesis of versatile peroxidase (from Pleurotus eryngii) allowed us to corroborate the computational analysis and the role played by the buried tryptophan (Trp244) and a neighbor phenylalanine residue (Phe198), together with the surface tryptophan, in the electron transfer. These three aromatic residues are highly conserved in all the sequences analyzed (up to a total of 169). The importance of the surface (Trp171) and buried (Trp251) tryptophan residues in lignin peroxidase has been also confirmed by directed mutagenesis of the Phanerochaete chrysosporium enzyme. Overall, the combined procedure identifies analogous electron transfer pathways in the long-range oxidation mechanism for both ligninolytic peroxidases, constituting a good example of how computational analysis avoids making extensive trial-error mutagenic experiments.

Official webpage of indox [ industrialoxidoreductases ]. Optimized oxidoreductases for medium and large scale industrial biotransformations. This project has received funding from the European Union’s Seventh Framework Programme for research, technological development and demonstration under Grant Agreement nº: FP7-KBBE-2013-7-613549. © indox 2013. Developed by garcíarincón