Optimized oxidoreductases for medium and large scale industrial biotransformations
CLOSE
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
CLOSE
Private area
User:


Password:

publications
Total records: 126
Pages:    1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21  

[ 2014 ] Pita M, Maté D, González-Pérez D, Shleev S, Fernández VM, Alcalde M, De Lacey AL Bioelectrochemical Oxidation of Water J. Am. Chem. Soc., 136: 5892-5895
[ 2014 ] Piumi F, Levasseur A, Navarro D, Zhou S, Macellaro G, Mathieu Y, Ropartz D, Ludwig R, Faulds CB, Record E A novel glucose dehydrogenase from the white-rot fungus Pycnoporus cinnabarinus: production in Aspergillus niger and physicochemical characterization of the recombinant enzyme. Appl. Microbiol. Biotechnol., 98: 10105-10118
[ 2014 ] Rico A, Rencoret J, del Río JC, Martínez AT, Gutiérrez A Pretreatment with laccase and a phenolic mediator degrades lignin and enhances saccharification of Eucalyptus feedstock Biotechnol. Biofuels, 7: 6
[ 2013 ] Babot ED, del Río JC, Kalum L, Martínez AT, Gutiérrez A Oxyfunctionalization of aliphatic compounds by a recombinant peroxygenase from Coprinopsis cinerea Biotechnol. Bioeng., 110: 2323-2332
[ 2013 ] Bey M, Zhou S, Poidevin L, Henrissat B, Coutinho PM, Berrin JG, Sigoillot JC Cello-oligosaccharide oxidation reveals differences between two lytic polysaccharide monooxygenases (family GH61) from Podospora anserina Appl. Environ. Microbiol., 79: 488-496
[ 2013 ] Carabajal M, Kellner H, Levin L, Jehmlich N, Hofrichter M, Ullrich R The secretome of Trametes versicolor grown on tomato juice medium and purification of the secreted oxidoreductases including a versatile peroxidase J. Biotech., 168: 15-23
year2013
Formation of a tyrosine adduct involved in lignin degradation by Trametopsis cervina lignin peroxidase: A novel peroxidase activation mechanism
Miki Y, Pogni R, Acebes S, Lucas F, Fernandez-Fueyo E, Baratto MC, Fernández MI, de los Ríos V, Ruiz-Dueñas FJ, Sinicropi A, Basosi R, Hammel KE, Guallar V, Martínez AT
Biochem. J., 452: 575-584
Lignin peroxidase (LiP) from Trametopsis cervina has an exposed catalytic tyrosine (Tyr-181)instead of the conserved tryptophan of other lignin-degrading peroxidases. Pristine LiP showed alag period in veratryl alcohol (VA) oxidation. However, LiP after turnover with H2O2/VA (VA-LiP)lacked this lag, and H2O2-pretreated LiP (H2O2-LiP) was inactive. MS analyses revealed that VALiPincludes one VA molecule covalently bound to the side-chain of Tyr-181, whereas H2O2-LiPcontains hydroxylated Tyr-181. No adduct is formed by the Y171N variant. Molecular dockingshowed that VA binding is favored by sandwich π stacking with Tyr-181 and Phe-89. EPRspectroscopy after peroxide activation of the pretreated LiPs showed other protein radicals than thetyrosine radical found in pristine LiP, which were assigned to a tyrosine/VA adduct radical in VALiPand a dihydroxyphenyalanine radical in H2O2-LiP. Both radicals are able to oxidize large lowredox-potential substrates, but H2O2-LiP is unable to oxidize high redox-potential substrates.Transient-state kinetics showed that the tyrosine/VA adduct strongly promotes (>100-fold)substrate oxidation by compound II, the rate-limiting step in catalysis. The novel activationmechanism is involved in ligninolysis, as demonstrated using lignin model substrates. This is thefirst report on autocatalytic modification, resulting in functional alteration, among class-IIperoxidases.
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