Search Results - "Biaso, Frédéric"

Discovery of fungal oligosaccharide-oxidising flavo-enzymes with previously unknown substrates, redox-activity profiles and interplay with LPMOs by Haddad Momeni, Majid, Fredslund, Folmer, Bissaro, Bastien, Raji, Olanrewaju, Vuong, Thu V., Meier, Sebastian, Nielsen, Tine Sofie, Lombard, Vincent, Guigliarelli, Bruno, Biaso, Frédéric, Haon, Mireille, Grisel, Sacha, Henrissat, Bernard, Welner, Ditte Hededam, Master, Emma R., Berrin, Jean-Guy, Abou Hachem, Maher

“…Oxidative plant cell-wall processing enzymes are of great importance in biology and biotechnology. Yet, our insight into the functional interplay amongst such…”
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Mutations in the coordination spheres of T1 Cu affect Cu2+-activation of the laccase from Thermus thermophilus by Clément, Romain, Wang, Xie, Biaso, Frédéric, Ilbert, Marianne, Mazurenko, Ievgen, Lojou, Elisabeth

“…Thermus thermophilus laccase belongs to the sub-class of multicopper oxidases that is activated by the extra binding of copper to a methionine-rich domain…”
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Single-domain flavoenzymes trigger lytic polysaccharide monooxygenases for oxidative degradation of cellulose by Garajova, Sona, Mathieu, Yann, Beccia, Maria Rosa, Bennati-Granier, Chloé, Biaso, Frédéric, Fanuel, Mathieu, Ropartz, David, Guigliarelli, Bruno, Record, Eric, Rogniaux, Hélène, Henrissat, Bernard, Berrin, Jean-Guy

“…The enzymatic conversion of plant biomass has been recently revolutionized by the discovery of lytic polysaccharide monooxygenases (LPMOs) that carry out…”
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Spectroscopic and Structural Characterization of Reduced Desulfovibrio vulgaris Hildenborough W‑FdhAB Reveals Stable Metal Coordination during Catalysis by Oliveira, Ana Rita, Mota, Cristiano, Klymanska, Kateryna, Biaso, Frédéric, Romão, Maria João, Guigliarelli, Bruno, Pereira, Inês Cardoso

“…Metal-dependent formate dehydrogenases are important enzymes due to their activity of CO2 reduction to formate. The tungsten-containing FdhAB formate…”
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Gating of Substrate Access and Long-Range Proton Transfer in Escherichia coli Nitrate Reductase A: The Essential Role of a Remote Glutamate Residue by Al-Attar, Sinan, Rendon, Julia, Sidore, Marlon, Duneau, Jean-Pierre, Seduk, Farida, Biaso, Frédéric, Grimaldi, Stéphane, Guigliarelli, Bruno, Magalon, Axel

“…The Mo/W-bisPGD enzyme superfamily comprises a vast number of mononuclear molybdenum and tungsten enzymes that catalyze a great diversity of vital reactions in…”
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Copper Complexes as Bioinspired Models for Lytic Polysaccharide Monooxygenases by Concia, Alda Lisa, Beccia, Maria Rosa, Orio, Maylis, Ferre, Francine Terra, Scarpellini, Marciela, Biaso, Frédéric, Guigliarelli, Bruno, Réglier, Marius, Simaan, A. Jalila

“…We report here two copper complexes as first functional models for lytic polysaccharide monooxygenases, mononuclear copper-containing enzymes involved in…”
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Structural insights into the semiquinone form of human Cytochrome P450 reductase by DEER distance measurements between a native flavin and a spin labelled non-canonical amino acid by Bizet, Maxime, Byrne, Deborah, Biaso, Frédéric, Gerbaud, Guillaume, Etienne, Emilien, Briola, Giuseppina, Guigliarelli, Bruno, Urban, Philippe, Dorlet, Pierre, Kalai, Tamas, Truan, Gilles, Martinho, Marlène

“…The flavoprotein Cytochrome P450 reductase (CPR) is the unique electron pathway from NADPH to Cytochrome P450 (CYPs). The conformational dynamics of human CPR…”
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DFT Investigation of the Molybdenum Cofactor in Periplasmic Nitrate Reductases: Structure of the Mo(V) EPR-Active Species by Biaso, Frédéric, Burlat, Bénédicte, Guigliarelli, Bruno

“…The periplasmic nitrate reductase NAP belongs to the DMSO reductase family that regroups molybdoenzymes housing a bis-molybdopterin cofactor as the active…”
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Membrane-Bound Flavocytochrome MsrQ Is a Substrate of the Flavin Reductase Fre in Escherichia coli by Caux, Christelle, Guigliarelli, Bruno, Vivès, Corinne, Biaso, Frédéric, Horeau, Marius, Hassoune, Hawra, Petit-Hartlein, Isabelle, Juillan-Binard, Céline, Torelli, Stephane, Fieschi, Franck, Nivière, Vincent

“…MsrPQ is a new type of methionine sulfoxide reductase (Msr) system found in bacteria. It is specifically involved in the repair of periplasmic methionine…”
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Tuning the redox properties of a [4Fe-4S] center to modulate the activity of Mo-bisPGD periplasmic nitrate reductase by Zeamari, Kamal, Gerbaud, Guillaume, Grosse, Sandrine, Fourmond, Vincent, Chaspoul, Florence, Biaso, Frédéric, Arnoux, Pascal, Sabaty, Monique, Pignol, David, Guigliarelli, Bruno, Burlat, Bénédicte

“…Molybdoenzymes are ubiquitous in living organisms and catalyze, for most of them, oxidation-reduction reactions using a large range of substrates. Periplasmic…”
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Structural evidence for a reaction intermediate mimic in the active site of a sulfite dehydrogenase by Djeghader, Ahmed, Rossotti, Melanie, Abdulkarim, Saleh, Biaso, Frédéric, Gerbaud, Guillaume, Nitschke, Wolfgang, Schoepp-Cothenet, Barbara, Soulimane, Tewfik, Grimaldi, Stéphane

“…By combining X-ray crystallography, electron paramagnetic resonance techniques and density functional theory-based modelling, we provide evidence for a direct…”
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Substrate-dependent oxidative inactivation of a W-dependent formate dehydrogenase involving selenocysteine displacement by Vilela-Alves, Guilherme, Manuel, Rita R, Viegas, Aldino, Carpentier, Philippe, Biaso, Frédéric, Guigliarelli, Bruno, Pereira, Inês A C, Romão, Maria João, Mota, Cristiano

“…Metal-dependent formate dehydrogenases are very promising targets for enzyme optimization and design of bio-inspired catalysts for CO reduction, towards…”
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Beyond the coupled distortion model: structural analysis of the single domain cupredoxin AcoP, a green mononuclear copper centre with original features by Roger, Magali, Leone, Philippe, Blackburn, Ninian J, Horrell, Sam, Chicano, Tadeo Moreno, Biaso, Frédéric, Giudici-Orticoni, Marie-Thérèse, Abriata, Luciano A, Hura, Greg L, Hough, Michael A, Sciara, Giuliano, Ilbert, Marianne

“…Cupredoxins are widely occurring copper-binding proteins with a typical Greek-key beta barrel fold. They are generally described as electron carriers that rely…”
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Spectroscopic characterization of a green copper site in a single-domain cupredoxin by Roger, Magali, Biaso, Frédéric, Castelle, Cindy J, Bauzan, Marielle, Chaspoul, Florence, Lojou, Elisabeth, Sciara, Giuliano, Caffarri, Stefano, Giudici-Orticoni, Marie-Thérèse, Ilbert, Marianne

“…Cupredoxins are widespread copper-binding proteins, mainly involved in electron transfer pathways. They display a typical rigid greek key motif consisting of…”
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Detrimental effect of the 6 His C-terminal tag on YedY enzymatic activity and influence of the TAT signal sequence on YedY synthesis by Sabaty, Monique, Grosse, Sandrine, Adryanczyk, Geraldine, Boiry, Séverine, Biaso, Frédéric, Arnoux, Pascal, Pignol, David

“…YedY, a molybdoenzyme belonging to the sulfite oxidase family, is found in most Gram-negative bacteria. It contains a twin-arginine signal sequence that is…”
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Impact of copper ligand mutations on a cupredoxin with a green copper center by Roger, Magali, Sciara, Giuliano, Biaso, Frédéric, Lojou, Elisabeth, Wang, Xie, Bauzan, Marielle, Giudici-Orticoni, Marie-Thérèse, Vila, Alejandro J., Ilbert, Marianne

“…Mononuclear cupredoxins contain a type 1 copper center with a trigonal or tetragonal geometry usually maintained by four ligands, a cystein, two histidines and…”
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Elucidating the Structures of the Low- and High-pH Mo(V) Species in Respiratory Nitrate Reductase: A Combined EPR, 14,15N HYSCORE, and DFT Study by Rendon, Julia, Biaso, Frédéric, Ceccaldi, Pierre, Toci, René, Seduk, Farida, Magalon, Axel, Guigliarelli, Bruno, Grimaldi, Stéphane

“…Respiratory nitrate reductases (Nars), members of the prokaryotic Mo/W-bis Pyranopterin Guanosine dinucleotide (Mo/W-bisPGD) enzyme superfamily, are key…”
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Reductive activation in periplasmic nitrate reductase involves chemical modifications of the Mo-cofactor beyond the first coordination sphere of the metal ion by Jacques, Julien G.J., Fourmond, Vincent, Arnoux, Pascal, Sabaty, Monique, Etienne, Emilien, Grosse, Sandrine, Biaso, Frédéric, Bertrand, Patrick, Pignol, David, Léger, Christophe, Guigliarelli, Bruno, Burlat, Bénédicte

“…In Rhodobacter sphaeroides periplasmic nitrate reductase NapAB, the major Mo(V) form (the “high g” species) in air-purified samples is inactive and requires…”
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Probing the Menasemiquinone Binding Mode to Nitrate Reductase A by Selective 2H and 15N Labeling, HYSCORE Spectroscopy, and DFT Modeling by Seif Eddine, Maryam, Biaso, Frédéric, Arias‐Cartin, Rodrigo, Pilet, Eric, Rendon, Julia, Lyubenova, Sevdalina, Seduk, Farida, Guigliarelli, Bruno, Magalon, Axel, Grimaldi, Stéphane

“…In vivo specific isotope labeling at the residue or substituent level is used to probe menasemiquinone (MSK) binding to the quinol oxidation site of…”
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New Trends in the Chemistry of Iron(III) Citrate Complexes: Correlations between X-ray Structures and Solution Species Probed by Electrospray Mass Spectrometry and Kinetics of Iron Uptake from Citrate by Iron Chelators by Gautier-Luneau, Isabelle, Merle, Claire, Phanon, Delphine, Lebrun, Colette, Biaso, Frédéric, Serratrice, Guy, Pierre, Jean-Louis

“…Despite the crucial role of “iron(III) citrate systems” in the iron metabolism of living organisms (bacteria as well as plants or mammals), the coordination…”
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