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Papers by angel martinez

International Microbiology, 2005

Wood is the main renewable material on Earth and is largely used as building material and in pape... more Wood is the main renewable material on Earth and is largely used as building material and in paper-pulp manufacturing. This review describes the composition of lignocellulosic materials, the different processes by which fungi are able to alter wood, including decay patterns caused by white, brown, and soft-rot fungi, and fungal staining of wood. The chemical, enzymatic, and molecular aspects of the fungal attack of lignin, which represents the key step in wood decay, are also discussed. Modern analytical techniques to investigate fungal degradation and modification of the lignin polymer are reviewed, as are the different oxidative enzymes (oxidoreductases) involved in lignin degradation. These include laccases, high redox potential ligninolytic peroxidases (lignin peroxidase, manganese peroxidase, and versatile peroxidase), and oxidases. Special emphasis is given to the reactions catalyzed, their synergistic action on lignin, and the structural bases for their unique catalytic prope...

Lignin-degrading basidiomycetes and related fungi produce heme-containing peroxidases and peroxyg... more Lignin-degrading basidiomycetes and related fungi produce heme-containing peroxidases and peroxygenases, avin-containing oxidases and dehydrogenases, and different copper-containing oxidoreductases. Heme peroxidases comprise classical ligninolytic peroxidases and new dye-decolorizing peroxidases, while heme peroxygenases belong to a still largely unexplored superfamily of heme-thiolate peroxidases. Nevertheless, basidiomycete unspeci c peroxygenases have the highest biotechnological interest due to their ability to catalyze a variety of regioand stereo-selective monooxygenation reactions with H2O2 as source of oxygen and nal electron acceptor. Flavooxidases are involved in both lignin and cellulose decay generating H2O2 that activates peroxidases and generates hydroxyl radical, respectively. The group of copper oxidoreductases also includes other H2O2 generating enzymes (copperradical oxidases), together with classical laccases that are the oxidoreductases with the largest number of...

The hospital branch has benefited from offering activities that use collections of imaging tests ... more The hospital branch has benefited from offering activities that use collections of imaging tests for specialists to use for decision-making in conjunction with other clinical examinations. It is intended to study pathologies resulting from cancer cells. In this article, there is the possibility of presenting Artificial Intelligence solutions to support specialists. For this, the objective is to use the concepts of Paraconsistent Logic and Artificial Intelligence applied in Artificial Neural Networks and to propose the use of components of Paraconsistent Artificial Neural Networks (PANN) to support specialists in decision-making. Keywords: Artificial Paraconsistent Neurons. Artificial Intelligence. Paraconsistent Logic. Deep Learning Paraconsistent. RESUMO O setor hospitalar se beneficiou de oferecer atividades que utilizam colecoes de testes de imagem para que os especialistas possam usar para tomar decisoes em conjunto com outros exames clinicos. O objetivo e estudar patologias res...

Journal of Fungi

Pleurotus eryngii is a grassland-inhabiting fungus of biotechnological interest due to its abilit... more Pleurotus eryngii is a grassland-inhabiting fungus of biotechnological interest due to its ability to colonize non-woody lignocellulosic material. Genomic, transcriptomic, exoproteomic, and metabolomic analyses were combined to explain the enzymatic aspects underlaying wheat–straw transformation. Up-regulated and constitutive glycoside–hydrolases, polysaccharide–lyases, and carbohydrate–esterases active on polysaccharides, laccases active on lignin, and a surprisingly high amount of constitutive/inducible aryl–alcohol oxidases (AAOs) constituted the suite of extracellular enzymes at early fungal growth. Higher enzyme diversity and abundance characterized the longer-term growth, with an array of oxidoreductases involved in depolymerization of both cellulose and lignin, which were often up-regulated since initial growth. These oxidative enzymes included lytic polysaccharide monooxygenases (LPMOs) acting on crystalline polysaccharides, cellobiose dehydrogenase involved in LPMO activati...

International Journal of Molecular Sciences

We aim to clarify the ligninolytic capabilities of dye-decolorizing peroxidases (DyPs) from bacte... more We aim to clarify the ligninolytic capabilities of dye-decolorizing peroxidases (DyPs) from bacteria and fungi, compared to fungal lignin peroxidase (LiP) and versatile peroxidase (VP). With this purpose, DyPs from Amycolatopsis sp., Thermomonospora curvata, and Auricularia auricula-judae, VP from Pleurotus eryngii, and LiP from Phanerochaete chrysosporium were produced, and their kinetic constants and reduction potentials determined. Sharp differences were found in the oxidation of nonphenolic simple (veratryl alcohol, VA) and dimeric (veratrylglycerol-β- guaiacyl ether, VGE) lignin model compounds, with LiP showing the highest catalytic efficiencies (around 15 and 200 s−1·mM−1 for VGE and VA, respectively), while the efficiency of the A. auricula-judae DyP was 1–3 orders of magnitude lower, and no activity was detected with the bacterial DyPs. VP and LiP also showed the highest reduction potential (1.28–1.33 V) in the rate-limiting step of the catalytic cycle (i.e., compound-II re...

Applied and environmental microbiology

Two laccase isoenzymes produced by Pleurotus eryngii were purified to electrophoretic homogeneity... more Two laccase isoenzymes produced by Pleurotus eryngii were purified to electrophoretic homogeneity (42- and 43-fold) with an overall yield of 56.3%. Laccases I and II from this fungus are monomeric glycoproteins with 7 and 1% carbohydrate content, molecular masses (by sodium dodecyl sulfate-polyacrylamide gel electrophoresis) of 65 and 61 kDa, and pIs of 4.1 and 4.2, respectively. The highest rate of 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonate) oxidation for laccase I was reached at 65 degrees C and pH 4, and that for laccase II was reached at 55 degrees C and pH 3.5. Both isoenzymes are stable at high pH, retaining 60 to 70% activity after 24 h from pH 8 to 12. Their amino acid compositions and N-terminal sequences were determined, the latter strongly differing from those of laccases of other basidiomycetes. Antibodies against laccase I reacted with laccase II, as well as with laccases from Pleurotus ostreatus, Pleurotus pulmonarius, and Pleurotus floridanus. Different hyd...

Catalysis Science & Technology

Some fungal peroxygenases (UPOs) selectively oxidize α-isophorone to 4-hydroxyisophorone (4HIP) a... more Some fungal peroxygenases (UPOs) selectively oxidize α-isophorone to 4-hydroxyisophorone (4HIP) and 4-ketoisophorone (4KIP) while others are less selective or unable.

ACS Catalysis

Unspecific peroxygenases (UPOs) are fungal secreted counterparts of the cytochrome P450 monooxyge... more Unspecific peroxygenases (UPOs) are fungal secreted counterparts of the cytochrome P450 monooxygenases present in most living cells. Both enzyme types share the ability to perform selective oxygenation reactions. Moreover, the Marasmius rotula UPO (MroUPO) catalyzes reactions of interest compared with the previously described UPOs, including formation of reactive epoxy fatty acids. To investigate substrate epoxidation, the most frequent positions of oleic acid at the MroUPO heme channel were predicted using binding and molecular dynamics simulations. Then, mutations in neighbor residues were designed aiming at modulating the enzyme epoxidation vs hydroxylation ratio. Both the native (wild-type recombinant) MroUPO and the mutated variants were expressed in Escherichia coli as active enzymes, and their action on oleic and other fatty acids was investigated by gas chromatography−mass spectrometry in combination with kinetic analyses. Interestingly, a small modification of the channel shape in the I153T variant increased the ratio between epoxidized oleic acid and its additionally hydroxylated derivatives. A fully opposite effect was attained with the double I153F/S156F variant that completely abolished the ability of the MroUPO to epoxidize oleic acid (while no activity was detected for the I153V variant). The rationale for these results was revealed by the substrate positioning in the above computational simulations, which predict a shorter distance between the oleic acid double bond and the oxygen atom of the peroxide-activated heme (compound I) in the I153T variant than in the native enzyme, promoting epoxidation. In contrast, the I153F/S156F double mutation fully prevents the approach of oleic acid in the bent conformation required for double-bond epoxidation, although its (sub)terminal hydroxylation was predicted and experimentally confirmed. The I153T mutation also increased the UPO selectivity on polyunsaturated fatty acid epoxidation, strongly reducing the ratio between simple epoxides and their hydroxylated derivatives, with respect to the native UPO.

Advances in Mathematics

In this paper we provide an integral representation of the fractional Laplace-Beltrami operator f... more In this paper we provide an integral representation of the fractional Laplace-Beltrami operator for general riemannian manifolds which has several interesting applications. We give two different proofs, in two different scenarios, of essentially the same result. One of them deals with compact manifolds with or without boundary, while the other approach treats the case of riemannian manifolds without boundary whose Ricci curvature is uniformly bounded below.

The Journal of biological chemistry, Jan 9, 2018

Peroxidases are considered essential agents of lignin degradation by white-rot basidiomycetes. Ho... more Peroxidases are considered essential agents of lignin degradation by white-rot basidiomycetes. However, low-molecular-weight oxidants likely have a primary role in lignin breakdown because many of these fungi delignify wood before its porosity has sufficiently increased for enzymes to infiltrate. It has been proposed that lignin peroxidases (LiPs, EC 1.11.1.14) fulfill this role by oxidizing the secreted fungal metabolite veratryl alcohol (VA) to its aryl cation radical (VA), releasing it to act as a one-electron lignin oxidant within woody plant cell walls. Here, we attached the fluorescent oxidant sensor BODIPY 581/591 throughout beads with a nominal porosity of 6 kDa and assessed whether peroxidase-generated aryl cation radical systems could oxidize the beads. As positive control, we used the 1,2,4,5-tetramethoxybenzene (TMB) cation radical, generated from TMB by horseradish peroxidase. This control oxidized the beads to depths that increased with the amount of oxidant supplied, ...

Biotechnology for biofuels, 2017

Floudas et al. (Science 336: 1715) established that lignin-degrading fungi appeared at the end of... more Floudas et al. (Science 336: 1715) established that lignin-degrading fungi appeared at the end of Carboniferous period associated with the production of the first ligninolytic peroxidases. Here, the subsequent evolution of these enzymes in Polyporales, where most wood-rotting fungi are included, is experimentally recreated using genomic information. With this purpose, we analyzed the evolutionary pathway leading to the most efficient lignin-degrading peroxidases characterizing Polyporales species. After sequence reconstruction from 113 genes of ten sequenced genomes, the main enzyme intermediates were resurrected and characterized. Biochemical changes were analyzed together with predicted sequences and structures, to understand how these enzymes acquired the ability to degrade lignin and how this ability changed with time. The most probable first peroxidase in Polyporales would be a manganese peroxidase (Mn(3+) oxidizing phenolic lignin) that did not change substantially until the a...

1A Jornadas Nacionales De Informacion Y Documentacion Sobre Economia Regional Del 23 Al 25 De Junio De 1988 1990 Isbn 84 505 9617 3 Pags 283 290, 1990

Biotechnology for Biofuels, 2016

Translational Behavioral Medicine, 2015

Advances in mobile technology and mobile applications (apps) have opened up an exciting new front... more Advances in mobile technology and mobile applications (apps) have opened up an exciting new frontier for behavioral health researchers, with a "second generation" of apps allowing for the simultaneous collection of multiple streams of data in real time. With this comes a host of technical decisions and ethical considerations unique to this evolving approach to research. Drawing on our experience developing a second-generation app for the simultaneous collection of text message, voice, and self-report data, we provide a framework for researchers interested in developing and using second-generation mobile apps to study health behaviors. Our Simplified Novel Application (SNApp) framework breaks the app development process into four phases: (1) information and resource gathering, (2) software and hardware decisions, (3) software development and testing, and (4) study start-up and implementation. At each phase, we address common challenges and ethical issues and make suggestions for effective and efficient app development. Our goal is to help researchers effectively balance priorities related to the function of the app with the realities of app development, human subjects issues, and project resource constraints.

PloS one, 2015

Versatile peroxidase (VP) from the white-rot fungus Pleurotus eryngii is a high redox potential p... more Versatile peroxidase (VP) from the white-rot fungus Pleurotus eryngii is a high redox potential peroxidase of biotechnological interest able to oxidize a wide range of recalcitrant substrates including lignin, phenolic and non-phenolic aromatic compounds and dyes. However, the relatively low stability towards pH of this and other fungal peroxidases is a drawback for their industrial application. A strategy based on the comparative analysis of the crystal structures of VP and the highly pH-stable manganese peroxidase (MnP4) from Pleurotus ostreatus was followed to improve the VP pH stability. Several interactions, including hydrogen bonds and salt bridges, and charged residues exposed to the solvent were identified as putatively contributing to the pH stability of MnP4. The eight amino acid residues responsible for these interactions and seven surface basic residues were introduced into VP by directed mutagenesis. Furthermore, two cysteines were also included to explore the effect of...

Journal of Biological Chemistry, 2015

Chem. Sci., 2015

Switchable site-selectivity through catalyst control is achieved in the direct functionalization ... more Switchable site-selectivity through catalyst control is achieved in the direct functionalization of picolinamides that contain two distinct C–H sites to construct diverse scaffolds from the same starting material.

The Journal of Physical Chemistry B, 2015

Peroxide-activated Auricularia auricula-judae dye-decolorizing peroxidase (DyP) forms a mixed Trp... more Peroxide-activated Auricularia auricula-judae dye-decolorizing peroxidase (DyP) forms a mixed Trp377 and Tyr337 radical, the former being responsible for oxidation of the typical DyP substrates (Linde et al. Biochem. J., 2015, 466, 253−262); however, a pure tryptophanyl radical EPR signal is detected at pH 7 (where the enzyme is inactive), in contrast with the mixed signal observed at pH for optimum activity, pH 3. On the contrary, the presence of a second tyrosine radical (at Tyr147) is deduced by a multifrequency EPR study of a variety of simple and double-directed variants (including substitution of the above and other tryptophan and tyrosine residues) at different freezing times after their activation by H 2 O 2 (at pH 3). This points out that subsidiary long-range electron-transfer pathways enter into operation when the main pathway(s) is removed by directed mutagenesis, with catalytic efficiencies progressively decreasing. Finally, self-reduction of the Trp377 neutral radical is observed when reaction time (before freezing) is increased in the absence of reducing substrates (from 10 to 60 s). Interestingly, the tryptophanyl radical is stable in the Y147S/Y337S variant, indicating that these two tyrosine residues are involved in the self-reduction reaction.

International Microbiology, 2005

Wood is the main renewable material on Earth and is largely used as building material and in pape... more Wood is the main renewable material on Earth and is largely used as building material and in paper-pulp manufacturing. This review describes the composition of lignocellulosic materials, the different processes by which fungi are able to alter wood, including decay patterns caused by white, brown, and soft-rot fungi, and fungal staining of wood. The chemical, enzymatic, and molecular aspects of the fungal attack of lignin, which represents the key step in wood decay, are also discussed. Modern analytical techniques to investigate fungal degradation and modification of the lignin polymer are reviewed, as are the different oxidative enzymes (oxidoreductases) involved in lignin degradation. These include laccases, high redox potential ligninolytic peroxidases (lignin peroxidase, manganese peroxidase, and versatile peroxidase), and oxidases. Special emphasis is given to the reactions catalyzed, their synergistic action on lignin, and the structural bases for their unique catalytic prope...

Lignin-degrading basidiomycetes and related fungi produce heme-containing peroxidases and peroxyg... more Lignin-degrading basidiomycetes and related fungi produce heme-containing peroxidases and peroxygenases, avin-containing oxidases and dehydrogenases, and different copper-containing oxidoreductases. Heme peroxidases comprise classical ligninolytic peroxidases and new dye-decolorizing peroxidases, while heme peroxygenases belong to a still largely unexplored superfamily of heme-thiolate peroxidases. Nevertheless, basidiomycete unspeci c peroxygenases have the highest biotechnological interest due to their ability to catalyze a variety of regioand stereo-selective monooxygenation reactions with H2O2 as source of oxygen and nal electron acceptor. Flavooxidases are involved in both lignin and cellulose decay generating H2O2 that activates peroxidases and generates hydroxyl radical, respectively. The group of copper oxidoreductases also includes other H2O2 generating enzymes (copperradical oxidases), together with classical laccases that are the oxidoreductases with the largest number of...

The hospital branch has benefited from offering activities that use collections of imaging tests ... more The hospital branch has benefited from offering activities that use collections of imaging tests for specialists to use for decision-making in conjunction with other clinical examinations. It is intended to study pathologies resulting from cancer cells. In this article, there is the possibility of presenting Artificial Intelligence solutions to support specialists. For this, the objective is to use the concepts of Paraconsistent Logic and Artificial Intelligence applied in Artificial Neural Networks and to propose the use of components of Paraconsistent Artificial Neural Networks (PANN) to support specialists in decision-making. Keywords: Artificial Paraconsistent Neurons. Artificial Intelligence. Paraconsistent Logic. Deep Learning Paraconsistent. RESUMO O setor hospitalar se beneficiou de oferecer atividades que utilizam colecoes de testes de imagem para que os especialistas possam usar para tomar decisoes em conjunto com outros exames clinicos. O objetivo e estudar patologias res...

Journal of Fungi

Pleurotus eryngii is a grassland-inhabiting fungus of biotechnological interest due to its abilit... more Pleurotus eryngii is a grassland-inhabiting fungus of biotechnological interest due to its ability to colonize non-woody lignocellulosic material. Genomic, transcriptomic, exoproteomic, and metabolomic analyses were combined to explain the enzymatic aspects underlaying wheat–straw transformation. Up-regulated and constitutive glycoside–hydrolases, polysaccharide–lyases, and carbohydrate–esterases active on polysaccharides, laccases active on lignin, and a surprisingly high amount of constitutive/inducible aryl–alcohol oxidases (AAOs) constituted the suite of extracellular enzymes at early fungal growth. Higher enzyme diversity and abundance characterized the longer-term growth, with an array of oxidoreductases involved in depolymerization of both cellulose and lignin, which were often up-regulated since initial growth. These oxidative enzymes included lytic polysaccharide monooxygenases (LPMOs) acting on crystalline polysaccharides, cellobiose dehydrogenase involved in LPMO activati...

International Journal of Molecular Sciences

We aim to clarify the ligninolytic capabilities of dye-decolorizing peroxidases (DyPs) from bacte... more We aim to clarify the ligninolytic capabilities of dye-decolorizing peroxidases (DyPs) from bacteria and fungi, compared to fungal lignin peroxidase (LiP) and versatile peroxidase (VP). With this purpose, DyPs from Amycolatopsis sp., Thermomonospora curvata, and Auricularia auricula-judae, VP from Pleurotus eryngii, and LiP from Phanerochaete chrysosporium were produced, and their kinetic constants and reduction potentials determined. Sharp differences were found in the oxidation of nonphenolic simple (veratryl alcohol, VA) and dimeric (veratrylglycerol-β- guaiacyl ether, VGE) lignin model compounds, with LiP showing the highest catalytic efficiencies (around 15 and 200 s−1·mM−1 for VGE and VA, respectively), while the efficiency of the A. auricula-judae DyP was 1–3 orders of magnitude lower, and no activity was detected with the bacterial DyPs. VP and LiP also showed the highest reduction potential (1.28–1.33 V) in the rate-limiting step of the catalytic cycle (i.e., compound-II re...

Applied and environmental microbiology

Two laccase isoenzymes produced by Pleurotus eryngii were purified to electrophoretic homogeneity... more Two laccase isoenzymes produced by Pleurotus eryngii were purified to electrophoretic homogeneity (42- and 43-fold) with an overall yield of 56.3%. Laccases I and II from this fungus are monomeric glycoproteins with 7 and 1% carbohydrate content, molecular masses (by sodium dodecyl sulfate-polyacrylamide gel electrophoresis) of 65 and 61 kDa, and pIs of 4.1 and 4.2, respectively. The highest rate of 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonate) oxidation for laccase I was reached at 65 degrees C and pH 4, and that for laccase II was reached at 55 degrees C and pH 3.5. Both isoenzymes are stable at high pH, retaining 60 to 70% activity after 24 h from pH 8 to 12. Their amino acid compositions and N-terminal sequences were determined, the latter strongly differing from those of laccases of other basidiomycetes. Antibodies against laccase I reacted with laccase II, as well as with laccases from Pleurotus ostreatus, Pleurotus pulmonarius, and Pleurotus floridanus. Different hyd...

Catalysis Science & Technology

Some fungal peroxygenases (UPOs) selectively oxidize α-isophorone to 4-hydroxyisophorone (4HIP) a... more Some fungal peroxygenases (UPOs) selectively oxidize α-isophorone to 4-hydroxyisophorone (4HIP) and 4-ketoisophorone (4KIP) while others are less selective or unable.

ACS Catalysis

Unspecific peroxygenases (UPOs) are fungal secreted counterparts of the cytochrome P450 monooxyge... more Unspecific peroxygenases (UPOs) are fungal secreted counterparts of the cytochrome P450 monooxygenases present in most living cells. Both enzyme types share the ability to perform selective oxygenation reactions. Moreover, the Marasmius rotula UPO (MroUPO) catalyzes reactions of interest compared with the previously described UPOs, including formation of reactive epoxy fatty acids. To investigate substrate epoxidation, the most frequent positions of oleic acid at the MroUPO heme channel were predicted using binding and molecular dynamics simulations. Then, mutations in neighbor residues were designed aiming at modulating the enzyme epoxidation vs hydroxylation ratio. Both the native (wild-type recombinant) MroUPO and the mutated variants were expressed in Escherichia coli as active enzymes, and their action on oleic and other fatty acids was investigated by gas chromatography−mass spectrometry in combination with kinetic analyses. Interestingly, a small modification of the channel shape in the I153T variant increased the ratio between epoxidized oleic acid and its additionally hydroxylated derivatives. A fully opposite effect was attained with the double I153F/S156F variant that completely abolished the ability of the MroUPO to epoxidize oleic acid (while no activity was detected for the I153V variant). The rationale for these results was revealed by the substrate positioning in the above computational simulations, which predict a shorter distance between the oleic acid double bond and the oxygen atom of the peroxide-activated heme (compound I) in the I153T variant than in the native enzyme, promoting epoxidation. In contrast, the I153F/S156F double mutation fully prevents the approach of oleic acid in the bent conformation required for double-bond epoxidation, although its (sub)terminal hydroxylation was predicted and experimentally confirmed. The I153T mutation also increased the UPO selectivity on polyunsaturated fatty acid epoxidation, strongly reducing the ratio between simple epoxides and their hydroxylated derivatives, with respect to the native UPO.

Advances in Mathematics

In this paper we provide an integral representation of the fractional Laplace-Beltrami operator f... more In this paper we provide an integral representation of the fractional Laplace-Beltrami operator for general riemannian manifolds which has several interesting applications. We give two different proofs, in two different scenarios, of essentially the same result. One of them deals with compact manifolds with or without boundary, while the other approach treats the case of riemannian manifolds without boundary whose Ricci curvature is uniformly bounded below.

The Journal of biological chemistry, Jan 9, 2018

Peroxidases are considered essential agents of lignin degradation by white-rot basidiomycetes. Ho... more Peroxidases are considered essential agents of lignin degradation by white-rot basidiomycetes. However, low-molecular-weight oxidants likely have a primary role in lignin breakdown because many of these fungi delignify wood before its porosity has sufficiently increased for enzymes to infiltrate. It has been proposed that lignin peroxidases (LiPs, EC 1.11.1.14) fulfill this role by oxidizing the secreted fungal metabolite veratryl alcohol (VA) to its aryl cation radical (VA), releasing it to act as a one-electron lignin oxidant within woody plant cell walls. Here, we attached the fluorescent oxidant sensor BODIPY 581/591 throughout beads with a nominal porosity of 6 kDa and assessed whether peroxidase-generated aryl cation radical systems could oxidize the beads. As positive control, we used the 1,2,4,5-tetramethoxybenzene (TMB) cation radical, generated from TMB by horseradish peroxidase. This control oxidized the beads to depths that increased with the amount of oxidant supplied, ...

Biotechnology for biofuels, 2017

Floudas et al. (Science 336: 1715) established that lignin-degrading fungi appeared at the end of... more Floudas et al. (Science 336: 1715) established that lignin-degrading fungi appeared at the end of Carboniferous period associated with the production of the first ligninolytic peroxidases. Here, the subsequent evolution of these enzymes in Polyporales, where most wood-rotting fungi are included, is experimentally recreated using genomic information. With this purpose, we analyzed the evolutionary pathway leading to the most efficient lignin-degrading peroxidases characterizing Polyporales species. After sequence reconstruction from 113 genes of ten sequenced genomes, the main enzyme intermediates were resurrected and characterized. Biochemical changes were analyzed together with predicted sequences and structures, to understand how these enzymes acquired the ability to degrade lignin and how this ability changed with time. The most probable first peroxidase in Polyporales would be a manganese peroxidase (Mn(3+) oxidizing phenolic lignin) that did not change substantially until the a...

1A Jornadas Nacionales De Informacion Y Documentacion Sobre Economia Regional Del 23 Al 25 De Junio De 1988 1990 Isbn 84 505 9617 3 Pags 283 290, 1990

Biotechnology for Biofuels, 2016

Translational Behavioral Medicine, 2015

Advances in mobile technology and mobile applications (apps) have opened up an exciting new front... more Advances in mobile technology and mobile applications (apps) have opened up an exciting new frontier for behavioral health researchers, with a "second generation" of apps allowing for the simultaneous collection of multiple streams of data in real time. With this comes a host of technical decisions and ethical considerations unique to this evolving approach to research. Drawing on our experience developing a second-generation app for the simultaneous collection of text message, voice, and self-report data, we provide a framework for researchers interested in developing and using second-generation mobile apps to study health behaviors. Our Simplified Novel Application (SNApp) framework breaks the app development process into four phases: (1) information and resource gathering, (2) software and hardware decisions, (3) software development and testing, and (4) study start-up and implementation. At each phase, we address common challenges and ethical issues and make suggestions for effective and efficient app development. Our goal is to help researchers effectively balance priorities related to the function of the app with the realities of app development, human subjects issues, and project resource constraints.

PloS one, 2015

Versatile peroxidase (VP) from the white-rot fungus Pleurotus eryngii is a high redox potential p... more Versatile peroxidase (VP) from the white-rot fungus Pleurotus eryngii is a high redox potential peroxidase of biotechnological interest able to oxidize a wide range of recalcitrant substrates including lignin, phenolic and non-phenolic aromatic compounds and dyes. However, the relatively low stability towards pH of this and other fungal peroxidases is a drawback for their industrial application. A strategy based on the comparative analysis of the crystal structures of VP and the highly pH-stable manganese peroxidase (MnP4) from Pleurotus ostreatus was followed to improve the VP pH stability. Several interactions, including hydrogen bonds and salt bridges, and charged residues exposed to the solvent were identified as putatively contributing to the pH stability of MnP4. The eight amino acid residues responsible for these interactions and seven surface basic residues were introduced into VP by directed mutagenesis. Furthermore, two cysteines were also included to explore the effect of...

Journal of Biological Chemistry, 2015

Chem. Sci., 2015

Switchable site-selectivity through catalyst control is achieved in the direct functionalization ... more Switchable site-selectivity through catalyst control is achieved in the direct functionalization of picolinamides that contain two distinct C–H sites to construct diverse scaffolds from the same starting material.

The Journal of Physical Chemistry B, 2015

Peroxide-activated Auricularia auricula-judae dye-decolorizing peroxidase (DyP) forms a mixed Trp... more Peroxide-activated Auricularia auricula-judae dye-decolorizing peroxidase (DyP) forms a mixed Trp377 and Tyr337 radical, the former being responsible for oxidation of the typical DyP substrates (Linde et al. Biochem. J., 2015, 466, 253−262); however, a pure tryptophanyl radical EPR signal is detected at pH 7 (where the enzyme is inactive), in contrast with the mixed signal observed at pH for optimum activity, pH 3. On the contrary, the presence of a second tyrosine radical (at Tyr147) is deduced by a multifrequency EPR study of a variety of simple and double-directed variants (including substitution of the above and other tryptophan and tyrosine residues) at different freezing times after their activation by H 2 O 2 (at pH 3). This points out that subsidiary long-range electron-transfer pathways enter into operation when the main pathway(s) is removed by directed mutagenesis, with catalytic efficiencies progressively decreasing. Finally, self-reduction of the Trp377 neutral radical is observed when reaction time (before freezing) is increased in the absence of reducing substrates (from 10 to 60 s). Interestingly, the tryptophanyl radical is stable in the Y147S/Y337S variant, indicating that these two tyrosine residues are involved in the self-reduction reaction.