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Accueil > Départements > Biochimie, Biophysique et Biologie Structurale > Pierre DORLET : Stress Oxydant et Détoxication

Publications de l’équipe

2017


  • L. Benkaidali, F. André, G. Moroy, B. Tangour, F. Maurel, et M. Petitjean, « The Cytochrome P450 3A4 Has Three Major Conformations: New Clues to Drug Recognition by this Promiscuous Enzyme », Molecular Informatics, 2017.
    Résumé : We computed the channels of the 3A4 isoform of the cytochrome P450 3A4 (CYP) on the basis of 24 crystal structures extracted from the Protein Data Bank (PDB). We identified three major conformations (denoted C, O1 and O2) using an enhanced version of the CCCPP software that we developed for the present work, while only two conformations (C and O(2) ) are considered in the literature. We established the flowchart of definition of these three conformations in function of the structural and physicochemical parameters of the ligand. The channels are characterized with qualitative and quantitative parameters, and not only with their surrounding secondary structures as it is usually done in the literature.
    Mots-clés : active site access channels, B3S, conformations, CYP 3A4 ligands, cytochromes P450, drug-drug interactions, LSOD.

  • M. Clémancey, T. Cantat, G. Blondin, J. - M. Latour, P. Dorlet, et G. Lefèvre, « Structural Insights into the Nature of Fe(0) and Fe(I) Low-Valent Species Obtained upon the Reduction of Iron Salts by Aryl Grignard Reagents », Inorganic Chemistry, vol. 56, nᵒ 7, p. 3834-3848, 2017.
    Résumé : Mechanistic studies of the reduction of Fe(III) and Fe(II) salts by aryl Grignard reagents in toluene/tetrahydrofuran mixtures in the absence of a supporting ligand, as well as structural insights regarding the nature of the low-valent iron species obtained at the end of this reduction process, are reported. It is shown that several reduction pathways can be followed, depending on the starting iron precursor. We demonstrate, moreover, that these pathways lead to a mixture of Fe(0) and Fe(I) complexes regardless of the nature of the precursor. Mössbauer and (1)H NMR spectroscopies suggest that diamagnetic 16-electron bisarene complexes such as (η(4)-C6H5Me)2Fe(0) can be formed as major species (85% of the overall iron quantity). The formation of a η(6)-arene-ligated low-spin Fe(I) complex as a minor species (accounting for ca. 15% of the overall iron quantity) is attested by Mössbauer spectroscopy, as well as by continuous-wave electron paramagnetic resonance (EPR) and pulsed-EPR (HYSCORE) spectroscopies. The nature of the Fe(I) coordination sphere is discussed by means of isotopic labeling experiments and density functional theory calculations. It is shown that the most likely low-spin Fe(I) candidate obtained in these systems is a diphenylarene-stabilized species [(η(6)-C6H5Me)Fe(I)Ph2](-) exhibiting an idealized C2v topology. This enlightens the nature of the lowest valence states accommodated by iron during the reduction of Fe(III) and Fe(II) salts by aryl Grignard reagents in the absence of any additional coligand, which so far remained rather unknown. The reactivity of these low-valent Fe(I) and Fe(0) complexes in aryl-heteroaryl Kumada cross-coupling conditions has also been investigated, and it is shown that the zerovalent Fe(0) species can be used efficiently as a precursor in this reaction, whereas the Fe(I) oxidation state does not exhibit any reactivity.
    Mots-clés : B3S, LSOD.


  • L. Dhers, N. Pietrancosta, L. Ducassou, B. Ramassamy, J. Dairou, M. Jaouen, F. André, D. Mansuy, et J. - L. Boucher, « Spectral and 3D model studies of the interaction of orphan human cytochrome P450 2U1 with substrates and ligands », Biochimica et Biophysica Acta (BBA) - General Subjects, vol. 1861, nᵒ 1, p. 3144-3153, 2017.

  • L. Ducassou, L. Dhers, G. Jonasson, N. Pietrancosta, J. - L. Boucher, D. Mansuy, et F. André, « Membrane-bound human orphan cytochrome P450 2U1: Sequence singularities, construction of a full 3D model, and substrate docking », Biochimie, vol. 140, p. 166-175, 2017.
    Résumé : BACKGROUND: Human cytochrome P450 2U1 (CYP2U1) is an orphan CYP that exhibits several distinctive characteristics among the 57 human CYPs with a highly conserved sequence in almost all living organisms. METHODS: We compared its protein sequence with those of the 57 human CYPs and constructed a 3D structure of a full-length CYP2U1 model bound to a POPC membrane. We also performed docking experiments of arachidonic acid (AA) and N-arachidonoylserotonin (AS) in this model. RESULTS: The protein sequence of CYP2U1 displayed two unique characteristics when compared to those of the human CYPs, the presence of a longer N-terminal region upstream of the putative trans-membrane helix (TMH) containing 8 proline residues, and of an insert of about 20 amino acids containing 5 arginine residues between helices A' and A. Its N-terminal part upstream of TMH involved an additional short terminal helix, in a manner similar to what was reported in the crystal structure of Saccharomyces cerevisiae CYP51. Our model also showed a specific interaction between the charged residues of insert AA' and phosphate groups of lipid polar heads, suggesting a possible role of this insert in substrate recruitment. Docking of AA and AS in this model showed these substrates in channel 2ac, with the terminal alkyl chain of AA or the indole ring of AS close to the heme, in agreement with the reported CYP2U1-catalyzed AA and AS hydroxylation regioselectivities. MAJOR CONCLUSION AND GENERAL SIGNIFICANCE: This model should be useful to find new endogenous or exogenous CYP2U1 substrates and to interpret the regioselectivity of their hydroxylation.
    Mots-clés : Access channels, Active site topology, Arachidonic acid, B3S, LSOD, Membrane interaction, molecular dynamics, N-arachidonoylserotonin.

  • N. El Bakkali-Tahéri, S. Tachon, M. Orio, S. Bertaina, M. Martinho, V. Robert, M. Réglier, T. Tron, P. Dorlet, et A. J. Simaan, « Characterization of Cu(II)-reconstituted ACC Oxidase using experimental and theoretical approaches », Archives of Biochemistry and Biophysics, 2017.
    Résumé : 1-Aminocyclopropane-1-carboxylic acid oxidase (ACCO) is a non heme iron(II) containing enzyme that catalyzes the final step of the ethylene biosynthesis in plants. The iron(II) ion is bound in a facial triad composed of two histidines and one aspartate (H177, D179 and H234). Several active site variants were generated to provide alternate binding motifs and the enzymes were reconstituted with copper(II). Continuous wave (cw) and pulsed Electron Paramagnetic Resonance (EPR) spectroscopies as well as Density Functional Theory (DFT) calculations were performed and models for the copper(II) binding sites were deduced. In all investigated enzymes, the copper ion is equatorially coordinated by the two histidine residues (H177 and H234) and probably two water molecules. The copper-containing enzymes are inactive, even when hydrogen peroxide is used in peroxide shunt approach. EPR experiments and DFT calculations were undertaken to investigate substrate's (ACC) binding on the copper ion and the results were used to rationalize the lack of copper-mediated activity.
    Mots-clés : ACC Oxidase, B3S, Copper, Density functional theory calculations, Electron paramagnetic resonance, Ethylene, LSOD.

  • H. Renault, M. De Marothy, G. Jonasson, P. Lara, D. R. Nelson, I. M. Nilsson, F. André, G. von Heijne, et D. Werck-Reichhart, « Gene duplication leads to altered membrane topology of a cytochrome P450 enzyme in seed plants », Molecular Biology and Evolution, 2017.
    Résumé : Evolution of the phenolic metabolism was critical for the transition of plants from water to land. A cytochrome P450, CYP73, with cinnamate 4-hydroxylase (C4H) activity, catalyzes the first plant-specific and rate-limiting step in this pathway. The CYP73 gene is absent from green algae, and first detected in bryophytes. A CYP73 duplication occurred in the ancestor of seed plants and was retained in Taxaceae and most angiosperms. In spite of a clear divergence in primary sequence, both paralogs can fulfill comparable cinnamate hydroxylase roles both in vitro and in vivo. One of them seems dedicated to the biosynthesis of lignin precursors. Its N-terminus forms a single membrane spanning helix and its properties and length are highly constrained. The second is characterized by an elongated and variable N-terminus, reminiscent of ancestral CYP73s. Using as proxies the Brachypodium distachyon proteins, we show that the elongation of the N-terminus does not result in an altered subcellular localization, but in a distinct membrane topology. Insertion in the membrane of endoplasmic reticulum via a double-spanning open hairpin structure allows reorientation to the lumen of the catalytic domain of the protein. In agreement with participation to a different functional unit and supramolecular organization, the protein displays altered heme proximal surface. These data suggest the evolution of divergent C4H enzymes feeding different branches of the phenolic network in seed plants. It shows that specialization required for retention of gene duplicates may result from altered protein topology rather than change in enzyme activity.
    Mots-clés : B3S, LSOD.


  • J. Santolini, F. André, S. Jeandroz, et D. Wendehenne, « Nitric oxide synthase in plants: Where do we stand? », Nitric Oxide, vol. 63, p. 30-38, 2017.


  • M. Weisslocker-Schaetzel, M. Lembrouk, J. Santolini, et P. Dorlet, « Revisiting the Val/Ile Mutation in Mammalian and Bacterial Nitric Oxide Synthases: A Spectroscopic and Kinetic Study », Biochemistry, vol. 56, nᵒ 5, p. 748-756, févr. 2017.

2016

2015

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2014

  1. Bakari, S., André, F., Seigneurin-Berny, D., Delaforge, M., Rolland, N., Frelet-Barrand, A. 2014. Lactococcus lactis, recent developments in functional expression of membrane proteins. In Membrane Proteins Production for Structural Analysis. I. Mus-Veteau, editor. Springer eBook.
  2. Benkaidali, L., André, F., Maouche, B., Siregar, P., Benyettou, M., Maurel, F., Petitjean, M. (2014). Computing cavities, channels, pores and pockets in proteins from non-spherical ligands models. Bioinformatics 30,792-800.
  3. Bonnot, F., Tremey, E., von Stetten, D., Rat, S., Duval, S., Carpentier, P., Clemancey, M., Desbois, A., Niviere, V. (2014). Formation of High-Valent Iron-Oxo Species in Superoxide Reductase : Characterization by Resonance Raman Spectroscopy. Angew Chem Int Ed Engl.
  4. Cabaret, O., Puel, O., Botterel, F., Delaforge, M., Bretagne, S. (2014). Metabolic detoxification pathways for 5-methoxy-sterigmatocystin in primary tracheal epithelial cells. Xenobiotica 44,1-9.
  5. Touati, W., Tran, T., Seguin, J., Diry, M., Flinois, J. P., Baillou, C., Lescaille, G., Andre, F., Tartour, E., Lemoine, F. M., Beaune, P., de Waziers, I. (2014). A suicide gene therapy combining the improvement of cyclophosphamide tumor cytotoxicity and the development of an anti-tumor immune response. Curr Gene Ther 14,236-246.

2010

  1. Cabaret, O., Puel, O., Botterel, F., Pean, M., Khoufache, K., Costa, J. M., Delaforge, M., Bretagne, S. (2010). Metabolic detoxication pathways for sterigmatocystin in primary tracheal epithelial cells. Chem Res Toxicol 23,1673-1681.
  2. Duca, R. C., Badea, I. A., David, I. G., Delaforge, M., Vladescu, L. (2010). Redox behaviour of Zearalenone in various solvents. Anal Lett 43,1287-1300.
  3. Frelet-Barrand, A., Boutigny, S., Kunji, E. R., Rolland, N. (2010). Membrane protein expression in Lactococcus lactis. Methods Mol Biol 601,67-85.
  4. Frelet-Barrand, A., Boutigny, S., Moyet, L., Deniaud, A., Seigneurin-Berny, D., Salvi, D., Bernaudat, F., Richaud, P., Pebay-Peyroula, E., Joyard, J., Rolland, N. (2010). Lactococcus lactis, an alternative system for functional expression of peripheral and intrinsic Arabidopsis membrane proteins. PLoS One 5,e8746.
  5. Garcia, L., Maisonneuve, S., Xie, J., Guillot, R., Dorlet, P., Riviere, E., Desmadril, M., Lambert, F., Policar, C. (2010). Sugars to control ligand shape in metal complexes : conformationally constrained glycoligands with a predetermination of stereochemistry and a structural control. Inorg Chem 49,7282-7288.
  6. Giroud, C., Moreau, M., Mattioli, T. A., Balland, V., Boucher, J. L., Xu-Li, Y., Stuehr, D. J., Santolini, J. (2010). Role of arginine guanidinium moiety in nitric-oxide synthase mechanism of oxygen activation. J Biol Chem 285,7233-7245.
  7. Marechal, A., Mattioli, T. A., Stuehr, D. J., Santolini, J. (2010). NO synthase isoforms specifically modify peroxynitrite reactivity. FEBS J 277,3963-3973.
  8. Uyeda, G., Williams, J. C., Roman, M., Mattioli, T. A., Allen, J. P. (2010). The influence of hydrogen bonds on the electronic structure of light-harvesting complexes from photosynthetic bacteria. Biochemistry 49,1146-1159.
  9. Videau, O., Delaforge, M., Levi, M., Thevenot, E., Gal, O., Becquemont, L., Beaune, P., Benech, H. (2010). Biochemical and analytical development of the CIME cocktail for drug fate assessment in humans. Rapid Commun Mass Spectrom 24,2407-2419.

2013

  1. Bussy, U., Delaforge, M., El-Bekkali, C., Ferchaud-Roucher, V., Krempf, M., Tea, I., Galland, N., Jacquemin, D., Boujtita, M. (2013). Acebutolol and alprenolol metabolism predictions : comparative study of electrochemical and cytochrome P450-catalyzed reactions using liquid chromatography coupled to high-resolution mass spectrometry. Analytical and Bioanalytical Chemistry 405,6077-6085.
  2. Cano, P. M., Jamin, E. L., Tadrist, S., Bourdaud’hui, P., Pean, M., Debrauwer, L., Oswald, I. P., Delaforge, M., Puel, O. (2013). New untargeted metabolic profiling combining mass spectrometry and isotopic labeling : application on Aspergillus fumigatus grown on wheat. Anal. Chem. 85,8412-8420.
  3. El Ghachtouli, S., Vincent Ching, H. Y., Lassalle-Kaiser, B., Guillot, R., Leto, D. F., Chattopadhyay, S., Jackson, T. A., Dorlet, P., Anxolabehere-Mallart, E. (2013). Electrochemical formation of Mn(III)-peroxo complexes supported by pentadentate amino pyridine and imidazole ligands. Chem Commun 49,5696-5698.
  4. Gaibelet, G., Terce, F., Bertrand-Michel, J., Allart, S., Azalbert, V., Lecompte, M. F., Collet, X., Orlowski, S. (2013). 21-Methylpyrenyl-cholesterol stably and specifically associates with lipoprotein peripheral hemi-membrane : A new labelling tool. Biochem. Biophys. Res. Commun. 440,533-538.
  5. Hofer, R., Dong, L. M., Andre, F., Ginglinger, J. F., Lugan, R., Gavira, C., Grec, S., Lang, G., Memelink, J., Van der Krol, S., Bouwmeester, H., Werck-Reichhart, D. (2013). Geraniol hydroxylase and hydroxygeraniol oxidase activities of the CYP76 family of cytochrome P450 enzymes and potential for engineering the early steps of the (seco)iridoid pathway. Metab. Eng. 20,221-232.
  6. Lambert, C., Beraldo, H., Lievre, N., Garnier-Suillerot, A., Dorlet, P., Salerno, M. (2013). Bis(thiosemicarbazone) copper complexes : mechanism of intracellular accumulation. J Biol Inorg Chem 18,59-69.
  7. Santolini, J., Marechal, A., Boussac, A., Dorlet, P. (2013). EPR characterization of the ferrous nitrosyl complex formed within the oxygenase domain of NO-synthase. ChemBioChem 14,1852-1857.

2012

  1. Bellanger, A. P., Roussel, A., Millon, L., Delaforge, M., Reboux, G. (2012). Jewelry boxes contaminated by Aspergillus oryzae : an occupational health risk ? J Occup Environ Hyg 9,460-466.
  2. Bernad, S., Brunel, A., Dorlet, P., Sicard-Roselli, C., Santolini, J. (2012). A novel cryo-reduction method to investigate the molecular mechanism of nitric oxide synthases. J. Phys. Chem. B 116,5595-5603.
  3. Brunel, A., Santolini, J., Dorlet, P. (2012). EPR characterization of tetrahydrobiopterin radical formation in bacterial NOS compared to mammalian NOS. Biophys. J. 103,109-117.
  4. Deniaud, A., Panwar, P., Frelet-Barrand, A., Bernaudat, F., Juillan-Binard, C., Ebel, C., Rolland, N., Pebay-Peyroula, E. (2012). Oligomeric status and nucleotide binding properties of the plastid ATP/ADP transporter 1 : toward a molecular understanding of the transport mechanism. PLoS One 7,e32325.
  5. Duca, R. C., Mabondzo, A., Bravin, F., Delaforge, M. (2012). In vivo effects of zearalenone on the expression of proteins involved in the detoxification of rat xenobiotics. Environ Toxicol 27,98-108.
  6. El Ghachtouli, S., Guillot, R., Aukauloo, A., Dorlet, P., Anxolabehere-Mallart, E., Costentin, C. (2012). Hydroxide ion versus chloride and methoxide as an exogenous ligand reveals the influence of hydrogen bonding with second-sphere coordination water molecules in the electron transfer kinetics of Mn complexes. Inorg. Chem. 51,3603-3612.
  7. El Ghachtouli, S., Guillot, R., Dorlet, P., Anxolabéhère-Mallart, E., Aukauloo, A. (2012). Influence of second sphere hydrogen bonding interaction on a manganese(II)-aquo complex. Dalton Trans. 41,1675-1677.
  8. Faller, P., Hureau, C., Dorlet, P., Hellwig, P., Coppel, Y., Collin, F., Alies, B. (2012). Methods and techniques to study the bioinorganic chemistry of metal-peptide complexes linked to neurodegenerative diseases. Coord. Chem. Rev. 256,2381-2396.
  9. Hannibal, L., Collins, D., Brassard, J., Chakravarti, R., Vempati, R., Dorlet, P., Santolini, J., Dawson, J. H., Stuehr, D. J. (2012). Heme binding properties of glyceraldehyde-3-phosphate dehydrogenase. Biochemistry 51,8514-8529.
  10. Hureau, C., Dorlet, P. (2012). Coordination of redox active metal ions to the amyloid precursor protein and to amyloid-b peptides involved in Alzheimer disease. Part 2 : Dependence of Cu(II) binding sites with Ab sequences. Coord. Chem. Rev. 256,2175-2187.
  11. Kwiecien, R. A., Kosieradzka, K., Le Questel, J. Y., Lebreton, J., Fournial, A., Gentil, E., Delaforge, M., Paneth, P., Robins, R. J. (2012). Cytochrome P450 monooxygenase-catalyzed ring opening of the bicyclic amine, nortropine : an experimental and DFT computational study. Chem Cat Chem 4,530-539.
  12. Kwiecien, R. A., Le Questel, J. Y., Lebreton, J., Delaforge, M., Andre, F., Pihan, E., Roussel, A., Fournial, A., Paneth, P., Robins, R. J. (2012). Cytochrome P450-catalyzed degradation of nicotine : fundamental parameters determining hydroxylation by cytochrome P450 2A6 at the 5’-carbon or the N-methyl carbon. J Phys Chem B 116,7827-7840.
  13. Navascues, J., Perez-Rontones, C., Gay, M., Marcos, M., Yang, F., Walker, F. A., Desbois, A., Abian, J., Becana, M. (2012). Leghemoglobin green derivatives : heme nitration evidences production of highly reactive nitrogen species during aging of legume nodules Proc. Natl Acad. Sci. USA 109,2660-2665.
  14. Roussel, S., Reboux, G., Millon, L., Parchas, M. D., Boudih, S., Skana, F., Delaforge, M., Rakotonirainy, M. S. (2012). Microbiological evaluation of ten French archives and link to occupational symptoms. Indoor Air 22,514-522.
  15. Roussel, S., Reboux, G., Millon, L., Parchas, M. D., Vacheyrou, M., Boudih, S., Skana, F., Delaforge, M., Rakotonirainy, M. S. (2012). Rôle des enzymes du métabolisme des xénobiotiques dans la toxicité pulmonaire de deux mycotoxines d’Aspergillus versicolor et d’Aspergillus nidulans. J Mycol Med 22,111-112.
  16. Videau, O., Pitarque, S., Troncale, S., Hery, P., Thevenot, E., Delaforge, M., Benech, H. (2012). Can a cocktail designed for phenotyping pharmacokinetics and metabolism enzymes in human be used efficiently in rat ? Xenobiotica 42,349-354.
  17. Wang, Z. Q., Tejero, J., Wei, C. C., Haque, M. M., Santolini, J., Fadlalla, M., Biswas, A., Stuehr, D. J. (2012). Arg375 tunes tetrahydrobiopterin functions and modulates catalysis by inducible nitric oxide synthase. J. Inorg. Biochem. 108,203-215.

2011

  1. Bernaudat, F., Frelet-Barrand, A., Pochon, N., Dementin, S., Hivin, P., Boutigny, S., Rioux, J. B., Salvi, D., Seigneurin-Berny, D., Richaud, P., Joyard, J., Pignol, D., Sabaty, M., Desnos, T., Pebay-Peyroula, E., Darrouzet, E., Vernet, T., Rolland, N. (2011). Heterologous expression of membrane proteins : choosing the appropriate host. Plos One 6,e29191.
  2. Bessadok, A., Garcia, E., Jacquet, H., Martin, S., Garrigues, A., Loiseau, N., André, F., Orlowski, S., Vivaudou, M. (2011). Recognition of sulfonylurea receptor (ABCC8/9) ligands by the multidrug resistance transporter P-glycoprotein (ABCB1) : functional similarities based on common structural features between two multispecific ABC proteins. J. Biol. Chem. 286,3552-3569.
  3. Brunel, A., Wilson, A., Henry, L., Dorlet, P., Santolini, J. (2011). The proximal hydrogen bond network modulates Bacillus subtilis nitric-oxide synthase electronic and structural properties. J. Biol. Chem. 286,11997-12005.
  4. Cabaret, O., Puel, O., Botterel, F., Pean, M., Bretagne, S., Delaforge, M. (2011). Pulmonary metabolism of sterigmatocystin and methoxy-sterigmatocystin studies : contribution of uniformly 13C-enriched sterigmatocystin. J. Label Compd. Radiopharm. 54,287-288.
  5. Cabaret, O., Puel, O., Botterel, F., Pean, M., Bretagne, S., Delaforge, M. (2011). Contribution of uniformly 13C-enriched sterigmatocystin to the study of its pulmonary metabolism. Rapid Commun. Mass Spectrom. 25,2704-2710.
  6. Cox, N., Rapatskiy, L., Su, J. H., Pantazis, D. A., Sugiura, M., Kulik, L., Dorlet, P., Rutherford, A. W., Neese, F., Boussac, A., Lubitz, W., Messinger, J. (2011). Effect of Ca2+/Sr2+ substitution on the electronic structure of the oxygen-evolving complex of photosystem II : a combined multifrequency EPR, 55Mn-ENDOR, and DFT study of the S2 state. J. Am. Chem. Soc. 133,3635-3648.
  7. Deniaud, A., Bernaudat, F., Frelet-Barrand, A., Juillan-Binard, C., Vernet, T., Rolland, N., Pebay-Peyroula, E. (2011). Expression of a chloroplast ATP/ADP transporter in E. coli membranes : behind the Mistic strategy. Biochim. Biophys. Acta 1808,2059-2066.
  8. El Ghachtouli, S., Lassalle-Kaiser, B., Dorlet, P., Guillot, R., Anxolabéhère-Mallart, E., Costentin, C., Aukauloo, A. (2011). Implications of remote water molecules on the electron transfer coupled processes at a nonporphyrinic Mn(III)-hydroxido complex. Energy Environ. Sci. 4,2041-2044.
  9. El Khoury, Y., Dorlet, P., Faller, P., Hellwig, P. (2011). New insights into the coordination of Cu(II) by the Amyloid-b 16 peptide from Fourier transform IR spectroscopy and isotopic labeling. J. Phys. Chem. B 115,14812-14821.
  10. Geiger, R. A., Leto, D. F., Chattopadhyay, S., Dorlet, P., Anxolabehere-Mallart, E., Jackson, T. A. (2011). Geometric and electronic structures of peroxomanganese(III) complexes supported by pentadentate amino-pyridine and -imidazole ligands. Inorg. Chem. 50,10190-10203.
  11. Hureau, C., Eury, H., Guillot, R., Bijani, C., Sayen, S., Solari, P. L., Guillon, E., Faller, P., Dorlet, P. (2011). X-ray and solution structures of Cu(II) GHK and Cu(II) DAHK complexes : influence on their redox properties. Chem. Eur. J. 17,10151-10160.
  12. Jankowski, C. K., Chiasson, J. B., Dako, E., Doucet, K., Surette, M. E., André, F., Delaforge, M. (2011). Modeling of cytochrome P450 (Cyt P450, CYP) channels. Spectroscopy-Biomedical Applications 25,63-87.
  13. Lang, J., Santolini, J., Couture, M. (2011). The conserved Trp-Cys hydrogen bond dampens the "push effect" of the heme cysteinate proximal ligand during the first catalytic cycle of nitric oxide synthase. Biochemistry 50,10069-10081.
  14. Perrin, L., Loiseau, N., André, F., Delaforge, M. (2011). Metabolism of N-methyl-amide by cytochrome P450s. FEBS journal 278,2167-2178.
  15. Pinheiro, L., Buisson, D., Cortial, S., Delaforge, M., Ouazzani, J. (2011). Microbial decyanation of 1-benzylpyrrolidine-2,5-dicarbonitrile. Mechanistic investigations. J. Mol. Catal. B : Enzym. 68,211-215.
  16. Santolini, J. (2011). The molecular mechanism of mammalian NO-synthases : a story of electrons and protons. J. Inorg. Biochem. 105,127-141.
  17. Su, J. H., Cox, N., Ames, W., Pantazis, D. A., Rapatskiy, L., Lohmiller, T., Kulik, L. V., Dorlet, P., Rutherford, A. W., Neese, F., Boussac, A., Lubitz, W., Messinger, J. (2011). The electronic structures of the S2 states of the oxygen-evolving complexes of photosystem II in plants and cyanobacteria in the presence and absence of methanol. Biochim. Biophys. Acta 1807,829-840.

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