Optimized oxidoreductases for medium and large scale industrial biotransformations
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
Fax: 34 915360432
Mobile: 34 650080476
Private area


Total records: 112
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[ 2015 ] Fernandez-Fueyo E, Linde D, Almendral D, López-Lucendo MF, Ruiz-Dueñas FJ, Martínez AT Description of the first fungal dye-decolorizing peroxidase oxidizing manganese(II) Appl. Microbiol. Biotechnol., doi: 10.1007/s00253-015-6665-3
[ 2015 ] Fernandez-Fueyo E, van Wingerden M, Renirie R, Wever R, Ni Y, Holtmann D, Hollmann F Chemoenzymatic Halogenation of Phenols by using the Haloperoxidase from Curvularia inaequalis ChemCatChem, doi: 10.1002/cctc.201500862
[ 2015 ] Ferreira P, Carro J, Serrano A, Martínez AT A survey of genes encoding H2O2-producing GMC oxidoreductases in 10 Polyporales genomes Mycologia, 107: 1105-1119
[ 2015 ] Ferreira P, Hernández-Ortega A, Lucas F, Carro J, Herguedas B, Borrelli K, Guallar V, Martínez AT, Medina M Aromatic stacking interactions govern catalysis in aryl-alcohol oxidase FEBS J., 282: 3091-3106
[ 2015 ] Hofrichter M, Kellner H, Pecyna MJ, Ullrich R Fungal unspecific peroxygenases: heme-thiolate proteins that combine peroxidase and cytochrome p450 properties Adv. Exp. Med. Biol., 851: 341-368
[ 2015 ] Kracher D, Zahma K, Schulz C, Sygmund C, Gorton L, Ludwig R Inter-domain electron transfer in cellobiose dehydrogenase: modulation by pH and divalent cations FEBS J., doi: 10.1111/febs.13310
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