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613 results on '"Fantucci, P."'

1. N-Acetylcysteine Antagonizes NGF Activation of TrkA through Disulfide Bridge Interaction, an Effect Which May Contribute to Its Analgesic Activity

Author

Govoni, S, Fantucci, P, Marchesi, N, Vertemara, J, Pascale, A, Allegri, M, Calvillo, L, Vanoli, E, Govoni S., Fantucci P., Marchesi N., Vertemara J., Pascale A., Allegri M., Calvillo L., Vanoli E., Govoni, S, Fantucci, P, Marchesi, N, Vertemara, J, Pascale, A, Allegri, M, Calvillo, L, Vanoli, E, Govoni S., Fantucci P., Marchesi N., Vertemara J., Pascale A., Allegri M., Calvillo L., and Vanoli E.

Abstract

N-acetylcysteine (NAC), a mucolytic agent and an antidote to acetaminophen intoxication, has been studied in experimental conditions and trials exploring its analgesic activity based on its antioxidant and anti-inflammatory properties. The purpose of this study is to investigate additional mechanisms, namely, the inhibition of nerve growth factor (NGF) and the activation of the Tropomyosin receptor kinase A (TrkA) receptor, which is responsible for nociception. In silico studies were conducted to evaluate dithiothreitol and NAC’s interaction with TrkA. We also measured the autophosphorylation of TrkA in SH-SY5Y cells via ELISA to assess NAC’s in vitro activity against NGF-induced TrkA activation. The in silico and in vitro tests show that NAC interferes with NGF-induced TrkA activation. In particular, NAC breaks the disulfide-bound Cys 300–345 of TrkA, perturbing the NGF-TrkA interaction and producing a rearrangement of the binding site, inducing a consequent loss of their molecular recognition and spatial reorganization, which are necessary for the induction of the autophosphorylation process. The latter was inhibited by 40% using 20 mM NAC. These findings suggest that NAC could have a role as a TrkA antagonist, an action that may contribute to the activity and use of NAC in various pain states (acute, chronic, nociplastic) sustained by NGF hyperactivity and/or accompanied by spinal cord sensitization.

Published
2024

5. Effects of Saccharomyces cerevisiae cell wall addition on feed digestibility, fecal fermentation and microbiota and immunological parameters in adult cats

Author

de Oliveira Matheus, Laura Fantucci, Risolia, Larissa Wunsche, Ernandes, Mariane Ceschin, de Souza, Johnny Maciel, Oba, Patrícia Massae, Vendramini, Thiago Henrique Annibale, Pedrinelli, Vivian, Henríquez, Lucas Ben Fiuza, de Oliveira Massoco, Cristina, Pontieri, Cristiana Fonseca Ferreira, and Brunetto, Marcio Antonio

Published
2021
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6. Recent Theoretical Insights into the Oxidative Degradation of Biopolymers and Plastics by Metalloenzymes

Author

Rovaletti, A, De Gioia, L, Fantucci, P, Greco, C, Vertemara, J, Zampella, G, Arrigoni, F, Bertini, L, Rovaletti, Anna, De Gioia, Luca, Fantucci, Piercarlo, Greco, Claudio, Vertemara, Jacopo, Zampella, Giuseppe, Arrigoni, Federica, Bertini, Luca, Rovaletti, A, De Gioia, L, Fantucci, P, Greco, C, Vertemara, J, Zampella, G, Arrigoni, F, Bertini, L, Rovaletti, Anna, De Gioia, Luca, Fantucci, Piercarlo, Greco, Claudio, Vertemara, Jacopo, Zampella, Giuseppe, Arrigoni, Federica, and Bertini, Luca

Abstract

Molecular modeling techniques have become indispensable in many fields of molecular sciences in which the details related to mechanisms and reactivity need to be studied at an atomistic level. This review article provides a collection of computational modeling works on a topic of enormous interest and urgent relevance: the properties of metalloenzymes involved in the degradation and valorization of natural biopolymers and synthetic plastics on the basis of both circular biofuel production and bioremediation strategies. In particular, we will focus on lytic polysaccharide monooxygenase, laccases, and various heme peroxidases involved in the processing of polysaccharides, lignins, rubbers, and some synthetic polymers. Special attention will be dedicated to the interaction between these enzymes and their substrate studied at different levels of theory, starting from classical molecular docking and molecular dynamics techniques up to techniques based on quantum chemistry.

Published
2023

8. Smell loss associated with SARS-CoV-2 is not clinically different from other viruses: a multicenter cohort study.

Author

Menon Miyake, Marcel, Pereira Valera, Fabiana Cardoso, Bragança Martins, Ronaldo, Mattoso Compagnoni, Inaê, Zilio Fantucci, Marina, Batista Murashima, Adriana de Andrade, Costa Mendes da Silva, Lilian Eslaine, Melquiades de Lima, Thais, Oliveira de Souza, Maria Vitória, Rezende Melo, Stella, Lutaif Dolci, Ricardo Landini, Gomes Floriano, Caio, Correia de Campos, Carlos Augusto, Nakanishi, Marcio, Magalhães Freire, Gustavo Subtil, Lima Valente, André, Aurélio Fornazieri, Marco, Barbosa da Silva, José Lucas, Kanieski Anzolin, Lucas, and Abrão Issa, Maria Júlia

Published
2024
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12. Theoretical Concepts

Author

Bonačič-Koutecký, V., Fantucci, P., Koutecký, J., Jelski, D. A., George, T. F., Vienneau, J. M., Jones, R. O., Pastor, G. M., Bennemann, K. H., Müller, H., Fritsche, H.-G., Skala, L., Bjørnholm, S., Jarrold, M. F., Berry, R. S., Goldanskii, Vitalii I., editor, Schäfer, Fritz Peter, editor, Toennies, J. Peter, editor, Lotsch, Helmut K. V., editor, and Haberland, Hellmut, editor

Published
1994
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14. Quantum molecular interpretation of optical response properties of simple metal clusters

Author

Bonačić-Koutecký, V., Fantucci, P., Koutecký, J., Araki, H., editor, Brézin, E., editor, Ehlers, J., editor, Frisch, U., editor, Hepp, K., editor, Jaffe, R. L., editor, Kippenhahn, R., editor, Weidenmüller, H. A., editor, Wess, J., editor, Zittartz, J., editor, Beiglböck, W., editor, Schmidt, Rüdiger, editor, Lutz, Hans O., editor, and Dreizler, Reiner, editor

Published
1992
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18. First-Principles Calculations on Ni,Fe-Containing Carbon Monoxide Dehydrogenases Reveal Key Stereoelectronic Features for Binding and Release of CO2 to/from the C-Cluster

Author

Breglia, R, Arrigoni, F, Sensi, M, Greco, C, Fantucci, P, De Gioia, L, Bruschi, M, Breglia, Raffaella, Arrigoni, Federica, Sensi, Matteo, Greco, Claudio, Fantucci, Piercarlo, De Gioia, Luca, Bruschi, Maurizio, Breglia, R, Arrigoni, F, Sensi, M, Greco, C, Fantucci, P, De Gioia, L, Bruschi, M, Breglia, Raffaella, Arrigoni, Federica, Sensi, Matteo, Greco, Claudio, Fantucci, Piercarlo, De Gioia, Luca, and Bruschi, Maurizio

Abstract

In view of the depletion of fossil fuel reserves and climatic effects of greenhouse gas emissions, Ni,Fe-containing carbon monoxide dehydrogenase (Ni-CODH) enzymes have attracted increasing interest in recent years for their capability to selectively catalyze the reversible reduction of CO2 to CO (CO2 + 2H+ + 2e-⇌ CO + H2O). The possibility of converting the greenhouse gas CO2 into useful materials that can be used as synthetic building blocks or, remarkably, as carbon fuels makes Ni-CODH a very promising target for reverse-engineering studies. In this context, in order to provide insights into the chemical principles underlying the biological catalysis of CO2 activation and reduction, quantum mechanics calculations have been carried out in the framework of density functional theory (DFT) on different-sized models of the Ni-CODH active site. With the aim of uncovering which stereoelectronic properties of the active site (known as the C-cluster) are crucial for the efficient binding and release of CO2, different coordination modes of CO2 to different forms and redox states of the C-cluster have been investigated. The results obtained from this study highlight the key role of the protein environment in tuning the reactivity and the geometry of the C-cluster. In particular, the protonation state of His93 is found to be crucial for promoting the binding or the dissociation of CO2. The oxidation state of the C-cluster is also shown to be critical. CO2 binds to Cred2 according to a dissociative mechanism (i.e., CO2 binds to the C-cluster after the release of possible ligands from Feu) when His93 is doubly protonated. CO2 can also bind noncatalytically to Cred1 according to an associative mechanism (i.e., CO2 binding is preceded by the binding of H2O to Feu). Conversely, CO2 dissociates when His93 is singly protonated and the C-cluster is oxidized at least to the Cint redox state.

Published
2021

22. Ab initio adiabatic dynamics combined with wigner distribution approach to femtosecond pump-probe negative ion to neutral to positive ion (NeNePo) spectroscopy of Ag(sub)2Au, Ag(sub)4, and Au(sub)4 clusters

Author

Mitric, R., Hartmann, M., Stanca, B., Bonacic-Koutecky, V., and Fantucci, P.

Subjects
Chemistry, Physical and theoretical -- Research, Ions -- Analysis, Electrons -- Analysis, Spectral energy distribution -- Analysis, Molecular dynamics -- Research, Chemicals, plastics and rubber industries
Published
2001

25. Ni-Fe hydrogenases: a density functional theory study of active site models

Author

Gioia, L. De, Fantucci, P., Guigliarelli, B., and Bertrand, P.

Subjects
Metalloenzymes -- Research, Density functionals -- Usage, Binding sites (Biochemistry) -- Models, Chemistry
Abstract

Quantum mechanical computations were performed on Ni-Fe complexes modeling the active site of the dinuclear [Ni-Fe] cluster of hydrogenases. The goal of these computations was also to verify whether these active site models are energy-minima structures and whether their electronic properties are in agreement with available experimental information. Findings confirmed that in all the enzyme forms that have been identified spectroscopically, the Fe ion remains in the same valence state. Also, redox chemistry between these forms is not centered on only one of the metal ions but involves the whole cluster.

Published
1999

26. Abstracts of the 6th FECS Conference 1998 Lectures

Author

Rowland, F. Sherwood, Blake, Donald R., Larsen, B. R., Lindskog, Anne, Peterson, Peter J., Williams, W. Peter, Wallington, T. J., Pilling, M. J., Carslaw, N., Creasey, D. J., Heard, D. E., Jacobs, P., Lee, J., Lewis, A. C., McQuaid, J. B., Stockwell, William R., Frank, Hartmut, Sacco, P., Cocheo, V., Lynge, E., Andersen, A., Nilsson, R., Barlow, L., Pukkala, E., Nordlinder, R., Boffetta, P., Grandjean, P., Heikkil, P., Hürte, L. G., Jakobsson, R., Lundberg, I., Moen, B., Partanen, T., Riise, T., Borowiak, A., De Saeger, E., Schnitzler, K. G., Gravenhorst, G., Jacobi, H. W., Moelders, S., Lammel, G., Busch, G., Beese, F. O., Dentener, F. J., Feichter, J., Fraedrich, K., Roelofs, G. J., Friedrich, R., Reis, S., Voehringer, F., Simpson, D., Moussiopoulos, N., Sahm, P., Tourlou, P. M., Salmons, R., Papameletiou, D., Maqueda, J. M., Suhr, Per B., Bell, W., Paton-Walsh, C., Woods, P. T., Partridge, R. H., Slemr, J., Slemr, F., Schmidbauer, N., Ravishankara, A. R., Jenkin, Michael E., de Leeuw, G., van Eijk, A. M. J., Flossmann, A. I., Wobrock, W., Mestayer, P. G., Tranchant, B., Ljungström, E., Karlsson, R., Larsen, S. E., Roemer, M., Builtjes, P. J. H., Koffi, Brigitte, Koffi, Ernest N’Dri, De Saeger, Emile, Ro-Poulsen, H., Mikkelsen, T. N., Hummelshøj, P., Hovmand, M. F., Simoneit, Bernd R. T., van der Meulen, A., Meyer, Michael B., Berndt, T., Böge, O., Stratmann, F., Cass, Glen R., Harrison, Roy M., Shi, Ji Ping, Hoffmann, T., Warscheid, B., Bandur, R., Marggraf, U., Nigge, W., Kamens, Richard, Jang, Myoseon, Strommen, Mike, Chien, Chao-Jung, Leach, Keri, Ammann, M., Kalberer, M., Arens, F., Lavanchy, V., Gâggeler, H. W., Baltensperger, U., Davies, J. A., Cox, R. A., Alonso, S. García, Pastor, R. Pérez, Argüello, Gustavo A., Willner, Helge, Berndt, T., Böge, O., Bogillo, V. I., Pokrovskiy, V. A., Kuraev, O. V., Gozhyk, P. F., Bolzacchini, E., Bruschi, M., Fantucci, P., Meinardi, S., Orlandi, M., Rindone, B., Bolzacchini, Ezio, Bohn, Birger, Rindone, Bruno, Bruschi, Maurizo, Zetzsch, Cornelius, Brussol, C., Duane, M., Larsen, B., Carlier, P., Kotzias, D., Caracena, A. Baeza, Aznar, A. Miñana, Ferradás, E. González, Christensen, C. S., Skov, H., Hummelshøj, P., Jensen, N. O., Lohse, C., Cocheo, V., Sacco, P., Chatzis, C., Cocheo, V., Sacco, P., Boaretto, C., Quaglio, F., Zaratin, L., Pagani, D., Cocheo, L., Cocheo, Vincenzo, Asnar, Agustin Minana, Baldan, Annerita, Ballesta, Pascual P., Boaretto, Caterina, Caracena, Antonia B., Ferradas, Enrique Gonzalez, Gonzalez-Flesca, Nobert, Goelen, Eddie, Hansen, Asger B., Sacco, Paolo, De Saeger, Emile, Skov, Henrik, Consonni, V., Gramatica, P., Santagostino, A., Galvani, P., Bolzacchini, E., Consonni, Viviana, Gramatica, Paola, Todeschini, Roberto, Dippel, G., Reinhardt, H., Zellner, R., Dämmer, K., Bednarek, G., Breil, M., Zellner, R., Febo, A., Allegrini, I., Giliberti, C., Perrino, C., Fogg, P. G. T., Geiger, H., Barnes, I., Becker, K. H., Maurer, T., Geyskens, F., Bormans, R., Lambrechts, M., Goelen, E., Giese, Martina, Frank, Hartmut, Glasius, M., Hornung, P., Jacobsen, J. K., Klausen, H. S., Klitgaard, K. C., Møller, C. K., Petersen, A. P. F., Petersen, L. S., Wessel, S., Hansen, T. S., Lohse, C., Boaretto, E., Heinemeier, J., Glasius, M., Di Bella, D., Lahaniati, M., Calogirou, A., Jensen, N. R., Hjorth, J., Kotzias, D., Larsen, B. R., Gonzalez-Flesca, N., Cicolella, A., Bates, M., Bastin, E., Gurbanov, M. A., Akhmedly, K. M., Balayev, V. S., Haselmann, K. F., Ketola, R., Laturnus, F., Lauritsen, F. R., Grøn, C., Herrmann, H., Ervens, B., Reese, A., Umschlag, Th., Wicktor, F., Zellner, R., Herrmann, H., Umschlag, Th., Müller, K., Bolzacchini, E., Meinardi, S., Rindone, B., Jenkin, Michael E., Hayman, Garry D., Jensen, N. O., Courtney, M., Hummelshøj, P., Christensen, C. S., Larsen, B. R., Johnson, Matthew S., Hegelund, Flemming, Nelander, Bengt, Kirchner, Frank, Klotz, B., Barnes, Ian, Sørensen, S., Becker, K. H., Etzkorn, T., Platt, U., Wirtz, K., Martín-Reviejo, M., Laturnus, Frank, Martinez, E., Cabañas, B., Aranda, A., Martín, P., Salgado, S., Rodriguez, D., Masclet, P., Jaffrezo, J. L., Hillamo, R., Mellouki, A., Le Calvé, S., Le Bras, G., Moriarty, J., O’Donnell, S., Wenger, J., Sidebottom, H., Mingarrol, M. T. Bomboi, Cosin, S., Pastor, R. Pérez, Alonso, S. García, Sanz, M. J., Bravo, I., Gonzalez, D., Pérez, M. A., Mustafaev, Islam, Mammadova, Saida, Noda, J., Hallquist, M., Langer, S., Ljungström, E., Nohara, K., Kutsuna, S., Ibusuki, T., Oehme, Michael, Kölliker, Stephan, Brombacher, Stephan, Merz, Leo, Pastor, R. Pérez, Alonso, S. García, Cabezas, A. Quejido, Peeters, J., Vereecken, L., El Yazal, J., Pfeffer, Hans-Ulrich, Breuer, Ludger, Platz, J., Nielsen, O. J., Sehested, J., Wallington, T. J., Ball, J. C., Hurley, M. D., Straccia, A. M., Schneider, W. F., Pérez-Casany, M. P., Nebot-Gil, I., Sánchez-Marín, J., Putz, E., Folberth, G., Pfister, G., Weissflog, L., Elansky, N. P., Sørensen, Søren, Barnes, Ian, Becker, K. H., Shao, M., Heiden, A. C., Kley, D., Rockel, P., Wildt, J., Silva, G. V. A., Vasconcelos, M. T., Fernandes, E. O., Santos, A. M. S., Skov, Henrik, Hansen, Asger, Løfstrøm, Per, Lorenzen, Gitte, Stabel, J. R., Wolkoff, P., Pedersen, T., Strom, A. B., Skov, Henrik, Hertel, Ole, Jensen, Finn Palmgren, Hjorth, Jens, Galle, Bosse, Wallin, Svante, Theloke, J., Libuda, H. G., Zabel, F., Touaty, Muriel, Bonsang, Bernard, Ullerstam, M., Langer, S., Ljungström, E., Wenger, John, Bonard, Amélie, Manning, Marcus, Nolan, Sinéad, O’Sullivan, Niamh, Sidebottom, Howard, Wenger, John, Collins, Eoin, Moriarty, Jennie, O’Donnell, Sinéad, Sidebottom, Howard, Wenger, John, Collins, Eoin, Moriarty, Jennie, O’Donnell, Sinéad, Sidebottom, Howard, Wenger, John, Sidebottom, Howard, Chadwick, Paul, O’Leary, Barbara, Treacy, Jack, Wolkoff, Peder, Clausen, Per A., Wilkins, Cornelius K., Hougaard, Karin S., Nielsen, Gunnar D., Zilinskis, Viktors, Jansons, Guntis, Peksens, Aigars, Lazdins, Agris, Arinci, Y. V., Erdöl, N., Ekinci, E., Okutan, H., Manlafalioglu, I., Bakeas, Evangelos B., Siskos, Panayotis A., Viras, Loizos G., Smirnioudi, Vasiliki N., Bottenheim, Jan W., Biesenthal, Thomas, Gong, Wanmin, Makar, Paul, Delmas, Véronique, Menard, Tamara, Tatry, Véronique, Moussafir, Jacques, Thomas, Dominique, Coppalle, Alexis, Ellermann, Thomas, Hertel, Ole, Skov, Henrik, Frohn, Lise, Manscher, Ole H., Friis, Jørgen, Girgzdiene, Rasa, Girgzdys, Aloyzas, Gurevich, N. A., Gårdfeldt, Katarina, Langer, Sarka, Hermans, C., Vandaele, A. C., Carleer, M., Fally, S., Colin, R., Bernath, P. F., Jenouvrier, A., Coquart, B., Mérienne, M. -F., Hertel, Ole, Frohn, Lise, Skov, Henrik, Ellermann, Thomas, Huntrieser, H., Schlager, H., Feigl, C., Kemp, Kåre, Palmgren, Finn, Kiilsholm, Sissi, Rasmussen, Alix, Sørensen, Jens Havskov, Klemm, Otto, Lange, Holger, Larsen, René Wugt, Larsen, Niels Wessel, Nicolaisen, Flemming, Sørensen, Georg Ole, Beukes, Jon Are, Larsen, Poul Bo, Jensen, Steen Solvang, Fenger, Jes, de Leeuw, Gerrit, Kunz, Gerard, Cohen, Leo, Schlünzen, Heinke, Muller, Frank, Schulz, Michael, Tamm, Susanne, Geernaert, Gary, Hertel, Ole, Pedersen, Britta, Geernaert, Lise Lotte Sørensen, Lund, Søren, Vignati, Elisabetta, Jickells, Tim, Spokes, Lucinda, Matei, C., Jinga, O. A., Jinga, D. C., Moliner, R., Braekman-Danheux, C., Fontana, A., Suelves, I., Thieman, T., Vassilev, S., Skov, Henrik, Hertel, Ole, Zlatev, Zahari, Brandt, Jørgen, Bastrup-Birk, Annemarie, Ellermann, Thomas, Frohn, Lise, Vandaele, A. C., Hermans, C., Carleer, M., Tsouli, A., Colin, R., Windsperger, Andreas M., Turi, Kristina, Dworak, Oliver, Zellweger, C., Weingartner, E., Rüttimann, R., Hofer, P., Baltensperger, U., Ziv, A., Iakovleva, E., Palmgren, F., Berkovicz, R., Skov, H., Alastuey, A., Querol, X., Chaves, A., Lopez-Soler, A., Ruiz, C., Andrees, J. M., Allegrini, I., Febo, A., Giusto, M., Angeloni, M., Di Filippo, P., D’Innocenzio, F., Lepore, L., Marconi, A., Arshinov, M. Yu., Belan, B. D., Davydov, D. K., Kovaleskii, V. K., Plotinov, A. P., Pokrovskii, E. V., Sklyadneva, T. K., Tolmachev, G. N., Arshinov, M. Yu., Belan, B. D., Sklyadneva, T. K., Behnke, Wolfgang, Elend, Manfred, Krüger, Ulrich, Zetzsch, Cornelius, Belan, B. D., Arshinov, M. Yu., Davydov, D. K., Kovalevskii, V. K., Plotnikov, A. P., Pokrovskii, E. V., Rasskazchikova, T. M., Sklyadneva, T. K., Tolmachev, G. N., Belan, B. D., Arshinov, M. Yu., Simonenkov, D. V., Tolmachev, G. N., Bilde, Merete, Aker, Pamela M., Börensen, C., Kirchner, U., Scheer, V., Vogt, R., Ellermann, T., Geernaert, L. L. S., Pryor, S. C., Barthelmie, R. J., Feilberg, Anders, Nielsen, Torben, Kamens, Richard M., Freitas, M. C., Marques, A. P., Reis, M. A., Alves, L. C., Ilyinskikh, N. N., Ilyinskikh, I. N., Ilyinskikh, E. N., Johansen, Keld, Stavnsbjerg, Peter, Gabrielsson, Pär, Bak, Flemming, Andersen, Erik, Autrup, Herman, Kamens, Richard, Jang, Myoseon, Strommen, Michael, Leach, Keri, Kirchner, U., Scheer, V., Börensen, C., Vogt, R., Igor, Komov, Svjatoslav, Galiy, Anatoliy, Burlak, Komov, I. L., Istchenko, A. A., Lourenço, M. G., MacTavish, D., Sirois, A., Masclet, Pierre, Jaffrezo, Jean Luc, van der Meulen, A., Milukaite, A., Morkunas, V., Jurgutis, P., Mikelinskiene, A., Nielsen, Torben, Feilberg, Anders, Binderup, Mona Lise, Pineda, M., Palacios, J. M., Garcia, E., Cilleruelo, C., Moliner, R., Popovitcheva, O. B., Trukhin, M. E., Persiantseva, N. M., Buriko, Yu, Starik, A. M., Demirdjian, B., Suzanne, J., Probst, T. U., Rietz, B., Alfassi, Z. B., Pokrovskiy, V. A., Zenobi, R., Bogatyr’ov, V. M., Gun’ko, V. M., Querol, X., Alastuey, A., Lopez-Soler, A., Mantilla, E., Plana, F., Artiño, B., Rauterberg-Wulff, A., Israël, G. W., Rocha, Teresa A. P., Duarte, Armando C., Röhrl, Andreas, Lammel, Gerhard, Spindler, G., Müller, K., Herrmann, H., Strommen, Michael R., Vignati, Elisabetta, de Leeuw, Gerrit, and Berkowicz, Ruwim

Published
1998
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33. Comparison of the effects of corneal and lacrimal gland denervation on the lacrimal functional unit of rats.

Author

Faustino Barros, Jacqueline Ferreira, Saranzo Sant'Ana, Ariane Mirela, Cristina Dias, Lara, Batista Murashima, Adriana de Andrade, Costa Mendes da Silva, Lilian Eslaine, Zilio Fantucci, Marina, and Melani Rocha, Eduardo

Subjects
LACRIMAL apparatus, DRY eye syndromes, CORNEA, SENSORY ganglia, BENZALKONIUM chloride, EYE drops, DYSAUTONOMIA, CLUSTER headache
Abstract

Copyright of Arquivos Brasileiros de Oftalmologia is the property of Arquivos Brasileiros de Oftalmologia and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Published
2022
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36. Electronic structure and reactivity of dioxygen-platinum complexes: an ab initio MO-LCAO study

Author

Fantucci, P., Lolli, S., and Pizzotti, M.

Subjects
Platinum compounds -- Research, Electronic structure -- Analysis, Chemistry
Abstract

Ab initio Hartree-Fock calculation of the electronic structure of the complex (PH(3))(2) Pt(eta(super 2)-O(2)) reveal the strong nucleophilic character of coordinated dioxygen. This complex reacts with positively polarized hydrogen atoms to give hydrogen peroxide. IR measurements reveal a stepwise process of the reaction, involving an hydroperoxide intermediate, in an acid medium. Acidity of the reactants influences the energy released in the process and second step of protonation is more difficult than the first step.

Published
1994

37. Validation of the Connecticut olfactory test (CCCRC) adapted to Brazil

Author

Fenólio, Guilherme H.M., Anselmo-Lima, Wilma T., Tomazini, Gabriela C., Compagnoni, Inaê M., Amaral, Maria S.A. do, Fantucci, Marina Z., Peixoto, Pedro P.L., Guimarães, Alessandro F., Guimarães, Roberto E.S., Sakano, Eulália, Valera, Fabiana C.P., and Tamashiro, Edwin

Abstract

Olfactory changes are quite common in the population, causing a significant impact on the quality of life. Documentation of the olfactory function is essential for the diagnosis, treatment and follow-up of patients with inflammatory diseases of the upper airways, neurodegenerative diseases or viral infections. Among the different existing smell tests, the CCCRC is an inexpensive test, easy to apply, but it has not yet been evaluated on a large scale in the Brazilian population.

Published
2022
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43. Redox potentials of small inorganic radicals and hexa-aquo complexes of first-row transition metals in water: a dft study based on the grand canonical ensemble

Author

Arrigoni, F, Breglia, R, De Gioia, L, Bruschi, M, Fantucci, P, Arrigoni, F, Breglia, R, De Gioia, L, Bruschi, M, and Fantucci, P

Abstract

The potentials of redox systems involving nitrogen, oxygen, and metal ions of the first-row transition series have been computed according to the general approach of the grand canonical ensemble, which leads to the equilibrium value of the reduction potential via a (complete) sampling of configuration space at a given temperature. The approach is a single configuration approach in the sense that identical molecular structures are sampled for both the oxidized and reduced species considered in water solution. In this study, the solute and a cluster of 11-12 water molecules are treated explicitly at the same level of theory and embedded in a continuum solvent. The molecular energies are computed in the framework of the density functional theory. Our approach is basically different from the approach based on the ThermoDynamic Cycle involving gas-phase calculations of the electron affinity of the oxidized species, corrected by the differential hydration energy (obtained from continuum solvent models only) between oxidized and reduced forms. The calculated redox potentials are in agreement with the available experimental data much closer than other results so far presented in the literature. Our results are very satisfactory also in the case of the 3+/2+ redox states of the first-row transition metals, i.e., systems with a high positive charge for which enhanced effects of the solvent are expected.

Published
2019

44. Reactivation of the Ready and Unready Oxidized States of [NiFe]-Hydrogenases: Mechanistic Insights from DFT Calculations

Author

Breglia, R, Greco, C, Fantucci, P, De Gioia, L, Bruschi, M, Breglia, Raffaella, Greco, Claudio, Fantucci, Piercarlo, De Gioia, Luca, Bruschi, Maurizio, Breglia, R, Greco, C, Fantucci, P, De Gioia, L, Bruschi, M, Breglia, Raffaella, Greco, Claudio, Fantucci, Piercarlo, De Gioia, Luca, and Bruschi, Maurizio

Abstract

The apparently simple dihydrogen formation from protons and electrons (2H+ + 2e- ↔ H2) is one of the most challenging reactions in nature. It is catalyzed by metalloenzymes of amazing complexity, called hydrogenases. A better understanding of the chemistry of these enzymes, especially that of the [NiFe]-hydrogenases subgroup, has important implications for production of H2 as alternative sustainable fuel. In this work, reactivation mechanism of the oxidized and inactive Ni-B and Ni-A states of the [NiFe]-hydrogenases active site has been investigated using density functional theory. Results obtained from this study show that one-electron reduction and protonation of the active site promote the removal of the bridging hydroxide ligand contained in Ni-B and Ni-A. However, this process is sufficient to activate only the Ni-B state. H2 binding to the active site is required to convert Ni-A to the active Ni-SIa state. Here, we also propose a reasonable structure for the spectroscopically well-characterized Ni-SIr and Ni-SU species, formed respectively from the one-electron reduction of Ni-B and Ni-A. Ni-SIr, depending on the pH at which the reaction occurs, features a bridging hydroxide ligand or a water molecule terminally coordinated to the Ni atom, whereas in Ni-SU a water molecule is terminally coordinated to the Fe atom, and the Cys64 residue is oxidized to sulfenate. The sulfenate oxygen atom in the Ni-A state affects the stereoelectronic properties of the binuclear cluster by modifying the coordination geometry of Ni, and consequently, by switching the regiochemistry of H2O and H2 binding from the Ni to the Fe atom. This effect is predicted to be at the origin of the different reactivation kinetics of the oxidized and inactive Ni-B and Ni-A states

Published
2019

45. Limitations and advances in new treatments and future perspectives of corneal blindness.

Author

Antunes-Foschini, Rosalia, Adriano, Leidiane, Batista Murashima, Adriana de Andrade, Pires Barbosa, Amanda, Fernando Nominato, Luis, Cristina Dias, Lara, Zilio Fantucci, Marina, Marcos Garcia, Denny, Alves, Monica, and Melani Rocha, Eduardo

Subjects
CORNEAL transplantation, BLINDNESS, VITAMIN A, CORNEA injuries, WOUND healing, GROWTH factors
Abstract

Copyright of Arquivos Brasileiros de Oftalmologia is the property of Arquivos Brasileiros de Oftalmologia and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Published
2021
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47. Corneal blindness in Plato's cave: the acting forces to prevent and revert corneal opacity. Part I: epidemiology and new physiopathological concepts.

Author

Barbosa, Amanda Pires, Alves, Monica, Fortes Furtado, João Marcello, Adriano, Leidiane, Fernando Nominato, Luis, Cristina Dias, Lara, Zilio Fantucci, Marina, Batista Murashima, Adriana de Andrade, and Melani Rocha, Eduardo

Subjects
CORNEAL opacity, BLINDNESS, DRY eye syndromes, EPIDEMIOLOGY, ENDEMIC diseases
Abstract

Copyright of Arquivos Brasileiros de Oftalmologia is the property of Arquivos Brasileiros de Oftalmologia and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Published
2020
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48. Catalytic Mechanism of Fungal Lytic Polysaccharide Monooxygenases Investigated by First-Principles Calculations

Author

Bertini, L, Breglia, R, Lambrughi, M, Fantucci, P, De Gioia, L, Borsari, M, Sola, M, Bortolotti, C, Bruschi, M, Bortolotti, CA, Bertini, L, Breglia, R, Lambrughi, M, Fantucci, P, De Gioia, L, Borsari, M, Sola, M, Bortolotti, C, Bruschi, M, and Bortolotti, CA

Abstract

Lytic polysaccharide monooxygenases (LPMOs) are Cu-containing enzymes that facilitate the degradation of recalcitrant polysaccharides by the oxidative cleavage of glycosidic bonds. They are gaining rapidly increasing attention as key players in biomass conversion, especially for the production of second-generation biofuels. Elucidation of the detailed mechanism of the LPMO reaction is a major step toward the assessment and optimization of LPMO efficacy in industrial biotechnology, paving the way to utilization of sustainable fuel sources. Here, we used density functional theory calculations to study the reaction pathways suggested to date, exploiting a very large active-site model for a fungal AA9 LPMO and using a celloheptaose unit as a substrate mimic. We identify a copper oxyl intermediate as being responsible for H-atom abstraction from the substrate, followed by a rapid, water-assisted hydroxyl rebound, leading to substrate hydroxylation.

Published
2018

49. Theoretical investigation of aerobic and anaerobic oxidative inactivation of the [NiFe]-hydrogenase active site

Author

Breglia, R, Greco, C, Fantucci, P, De Gioia, L, Bruschi, M, Breglia, R, Greco, C, Fantucci, P, De Gioia, L, and Bruschi, M

Abstract

The extraordinary capability of [NiFe]-hydrogenases to catalyse the reversible interconversion of protons and electrons into dihydrogen (H2) has stimulated numerous experimental and theoretical studies addressing the direct utilization of these enzymes in H2 production processes. Unfortunately, the introduction of these natural H2-catalysts in biotechnological applications is limited by their inhibition under oxidising (aerobic and anaerobic) conditions. With the aim of contributing to overcome this limitation, we studied the oxidative inactivation mechanism of [NiFe]-hydrogenases by performing Density Functional Theory (DFT) calculations on a very large model of their active site in which all the amino acids forming the first and second coordination spheres of the NiFe cluster have been explicitly included. We identified an O2 molecule and two H2O molecules as sources of the two oxygen atoms that are inserted at the active site of the inactive forms of the enzyme (Ni-A and Ni-B) under aerobic and anaerobic conditions, respectively. Furthermore, our results support the experimental evidence that the Ni-A-to-Ni-B ratio strongly depends on the number of reducing equivalents available for the process and on the oxidizing conditions under which the reaction takes place

Published
2018

50. On the photochemistry of Fe2(edt)(CO)4(PMe3)2, a [FeFe]-hydrogenase model: A DFT/TDDFT investigation

Author

Bertini, L, Alberto, M, Arrigoni, F, Vertemara, J, Fantucci, P, Bruschi, M, Zampella, G, De Gioia, L, Alberto, Me, De Gioia, L., Bertini, L, Alberto, M, Arrigoni, F, Vertemara, J, Fantucci, P, Bruschi, M, Zampella, G, De Gioia, L, Alberto, Me, and De Gioia, L.

Abstract

The photochemistry of the [FeFe] hydrogenases model [Fe-2(edt)(CO)(4)(PMe3)(2)] (edt=1-2 ethane-dithiolate, (1) is investigated at Time-Dependent Density Functional Theory (TDDFT) level, focusing on the effect of the phosphine ligands on the early stages of the photodynamic of the system compared to that of the all CO model Fe-2(pdt)(CO)(6) (2) (pdt=1-3 propanedithiolate). We observed a role of the FeS charge transfer for the lower energy singlet transitions, unveiling a photoisomerization pathway between the lowest energy forms while the higher energy excitations are likely involved in the CO dissociation pathways. TDDFT shows that the average Fe-CO bond elongation in 1 is shorter than that observed in 2, providing the electronic structure rationale on the observation that diiron dithiolates are more photo-stable with respect to the CO photolysis than the all CO model. This is relevant for catalyst photo-stability and is an advantageous and thus desirable feature for practical applications of photo-hydrogen evolution

Published
2018

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