Institut de Chimie Moléculaire et des Matériaux d'Orsay

Detoxification of V-nerve agents assisted by a microperoxidase: new pathway revealed by the use of a relevant VX simulant. V. B. Da Silva, J.-P. Mahy, X. Brazzolotto, P.-Y. Renard, R. Ricoux, J. Legros, ChemBioChem, 2024, 25, e202400137

Encapsulation of Microperoxidase‐8 into MIL‐101(Cr/Fe) Nanoparticles: A New Biocatalyst for the Epoxidation of Styrene. X. Kesse, C. Sicard, N. Steunou, J.-P. Mahy, R. Ricoux, Eur. J. Inorg. Chem., 2023, 26, e202300040

Unprotected Amine Transfer Performed by Non-Heme Iron(II) Complexes. A. Boullé, A. Doumbia, J.-P. Mahy, F. Avenier, Chem. Commun., 2023, 59, 79-81

Les métalloenzymes artificielles : de la biocatalyse à la médecine. M. Beaumet, W. Ghattas, J.-P. Mahy, L'Act. Chim., 2022, 479, 61-65

Photocatalytic Hydrogen Production and Carbon Dioxide Reduction Catalyzed by an Artificial Cobalt Hemoprotein. G. A. O. Udry, L. Tiessler-Sala, E. Pugliese, A. Urvoas, Z. Halime, J.-D. Maréchal, J.-P. Mahy, R. Ricoux, Int. J. Mol. Sci., 2022, 23, 14640

An artificial metalloprotein with metal-adaptive coordination sites and Ni-dependent quercetinase activity. M. Beaumet, A. Dose, A. Bräuer, J.-P. Mahy, W. Ghattas, M. Groll, C. R. Hess, J. Inorg. Biochem., 2022, 235, 111914

Artificial enzymes for Diels-Alder reactions. W. Ghattas, J.-P. Mahy, M. Réglier, A. J. Simaan, ChemBioChem, 2021, 22, 443-459

Recent progress in the development of new artificial metalloenzymes as biocatalysts for selective oxidations and Diels-Alder reaction - Mini-Review. F. Avenier, W. Ghattas, R. Ricoux, J.-P. Mahy, Vietnam J. Chem., 2020, 58, 423-433

Binding of a Soluble meso-Tetraarylporphyrin to Human Galectin-7 Induces Oligomerization and Modulates Its Pro-Apoptotic Activity. Y. López De Los Santos, D. N. Bernard, P. Egesborg, M. Létourneau, C. Lafortune, M. J. Cuneo, A. Urvoas, D. Chatenet, J.-P. Mahy, Y. St-Pierre, R. Ricoux, N. Doucet, Biochemistry, 2020, 59, 4591-4600

Bioinspired Symmetrical and Unsymmetrical Diiron Complexes for Selective Oxidation Catalysis with Hydrogen Peroxide. A. Trehoux, R. Guillot, M. Clémancey, G. Blondin, J.-M. Latour, J.-P. Mahy, F. Avenier, Dalton Trans., 2020, 49, 16657-16661

An artificial hemoprotein with inducible peroxidase- and monooxygenase-like activities. K. Kariyawasam, T. Di Meo, F. Hammerer, M. Valerio-Lepiniec, G. Sciortino, J.-D. Maréchal, P. Minard, J.-P. Mahy, A. Urvoas, R. Ricoux, Chem. Eur. J., 2020, 26, 14929-14937

Characterization in Aqueous Medium of an FMN Semiquinone Radical Stabilized by the Enzyme-Like Microenvironment of a Modified Polyethyleneimine. Y. Chevalier, Y. L. T. Ki, C. Herrero, D. L. Nouen, J.-P. Mahy, J.-P. Goddard, F. Avenier, Org. Biomol. Chem., 2020, 18, 4386-4389

Aerobic Oxidation Catalyzed by Polyoxometalates Associated to an Artificial Reductase at Room Temperature and in Water. A. Naim, Y. Chevalier, Y. Bouzidi, P. Gairola, P. Mialane, A. Dolbecq, F. Avenier, J.-P. Mahy, Inorg. Chem. Frontiers, 2020, 7, 2362-2369

Artificial iron hydrogenase made by covalent grafting of Knölker's complex into xylanase: Application in asymmetric hydrogenation of an aryl ketone in water. K. Kariyawasam, W. Ghattas, Y. L. D. L. Santos, N. Doucet, S. Gaillard, J.-L. Renaud, F. Avenier, J.-P. Mahy, R. Ricoux, Biotechnol. Appl. Biochem., 2020, 67, 563-573

Encapsulation of Microperoxidase-8 in MIL-101(Cr)-X Nanoparticles: Influence of Metal-Organic Framework Functionalization on Enzymatic Immobilization and Catalytic Activity. E. Gkaniatsou, R. Ricoux, K. Kariyawasam, I. Stenger, B. Fan, N. Ayoub, S. Salas, G. Patriarche, C. Serre, J.-P. Mahy, N. Steunou, C. Sicard, ACS Appl. Nano Mater., 2020, 3, 3233-3243

Recent advances in the field of artificial hemoproteins: new efficient eco-compatible biocatalysts for nitrene- oxene- and carbene-transfer reactions. K. Kariyawasam, R. Ricoux, J.-P. Mahy, J. Porphyr. Phthalocyanines, 2019, 23, 1273-1285

CuII-Containing 1-Aminocyclopropane Carboxylic Acid Oxidase Is an Efficient Stereospecific Diels–Alderase. W. Ghattas, V. Dubosclard, S. Tachon, M. Beaumet, R. Guillot, M. Réglier, A. J. Simaan, J.-P. Mahy, Angew. Chem. Int. Ed., 2019, 58, 14605-14609

Enhancing microperoxidase activity and selectivity: immobilization in metal-organic frameworks. E. Gkaniatsou, C. Serre, J.-P. Mahy, N. Steunou, R. Ricoux, C. Sicard, J. Porphyr. Phthalocyanines, 2019, 23, 718-728

Functionalized Artificial Bidomain Proteins Based on an α-Solenoid Protein Repeat Scaffold: A New Class of Artificial Diels–Alderases. T. Di Meo, K. Kariyawasam, W. Ghattas, M. Valerio-Lepiniec, G. Sciortino, J.-D. Maréchal, P. Minard, J.-P. Mahy, A. Urvoas, R. Ricoux, ACS Omega, 2019, 4, 4437-4447

Selective Formation of an FeIVO or an FeIIIOOH Intermediate From Iron(II) and H2O2 : Controlled Heterolytic versus Homolytic Oxygen-Oxygen Bond Cleavage by the Second Coordination Sphere. K. Cheaib, M. Q. E. Mubarak, K. Sénéchal-David, C. Herrero, R. Guillot, M. Clémancey, J.-M. Latour, S. D. Visser, J.-P. Mahy, F. Banse, F. Avenier, Angew. Chem. Int. Ed., 2019, 58, 854-858

Prix Nobel de Chimie 2018 : des chimistes qui dirigent l’évolution au profit de l’humain. W. Ghattas, J.-P. Mahy, L'Act. Chim., 2018, 435, 7-8

Incorporation of a minimal nucleotide into DNA. P. Röthlisberger, F. Levi-Acobas, I. Sarac, R. Ricoux, J.-P. Mahy, P. Herdewijn, P. Marlière, M. Hollenstein, Tetrahedron Lett., 2018, 59, 4241-4244

Aerobic Baeyer-Villiger Oxidation Catalyzed by a Flavin-Containing Enzyme Mimic in Water. Y. Chevalier, Y. L. T. Ki, D. L. Nouen, J.-P. Mahy, J.-P. Goddard, F. Avenier, Angew. Chem. Int. Ed., 2018, 57, 16412-16415

Enzyme encapsulation in mesoporous Metal-Organic Frameworks for selective biodegradation of harmful dye molecules. E. Gkaniatsou, C. Sicard, R. Ricoux, L. Benahmed, F. Bourdreux, Q. Zhang, C. Serre, J.-P. Mahy, N. Steunou, Angew. Chem. Int. Ed., 2018, 57, 16141-16146

Receptor-based artificial metalloenzymes on living human cells. W. Ghattas, V. Dubosclard, A. Wick, A. Bendelac, R. Guillot, R. Ricoux, J.-P. Mahy, J. Am. Chem. Soc., 2018, 140, 8756-8762

Imidazolidine Ring Cleavage upon Complexation with First Row Transition Metals. K. Cheaib, C. Herrero, R. Guillot, F. Banse, J.-P. Mahy, F. Avenier, Eur. J. Inorg. Chem., 2017, 3884-3891

αRep A3: A versatile artificial scaffold for metalloenzyme design. T. Di Meo, W. Ghattas, C. Herrero, C. Velours, P. Minard, J.-P. Mahy, R. Ricoux, A. Urvoas, Chem. Eur. J., 2017, 23, 10156-10166

Elucidating the light-induced charge accumulation in an artificial analogue of methane monooxygenase enzymes using time-resolved x-ray absorption spectroscopy. D. Moonshiram, A. Picon, Á. Vázquez-Mayagoitia, X. Zhang, M.-F. Tu, P. Garrido-Barros, J.-P. Mahy, F. Avenier, A. Aukauloo, Chem. Commun., 2017, 53, 2725-2728

Metal–organic frameworks: a novel host platform for enzymatic catalysis and detection. E. Gkaniatsou, C. Sicard, R. Ricoux, J.-P. Mahy, N. Steunou, C. Serre, Mater. Horiz., 2017, 4, 55-63

Photoassisted Oxidation of Sulfides Catalyzed by Artificial Metalloenzymes Using Water as an Oxygen Source. C. Herrero, N. Nguyen-Thi, F. Hammerer, F. Banse, D. Gagné, N. Doucet, J.-P. Mahy, R. Ricoux, Catalysts, 2016, 6, 202

Reduction of a Tris(picolyl)amine Copper(II) Complex by an Polymeric Flavo-Reductase model in Water. K. Cheaib, Y. Roux, C. Herrero, A. Trehoux, F. Avenier, J.-P. Mahy, Dalton Trans., 2016, 45, 18098-18101

A growing family of o2 activating dinuclear iron enzymes with key catalytic diiron(III)-peroxo intermediates: biological systems and chemical models. A. Trehoux, J.-P. Mahy, F. Avenier, Coord. Chem. Rev., 2016, 322, 142-158

Artificial Metalloenzymes with the Neocarzinostatin Scaffold: Toward a Biocatalyst for the Diels–Alder Reaction. W. Ghattas, L. Cotchico-Alonso, J.-D. Maréchal, A. Urvoas, M. Rousseau, J.-P. Mahy, R. Ricoux, ChemBioChem, 2016, 17, 433-440

Oxidation catalysis via visible-light water activation of a [Ru(bpy)3]2+ chromophore BSA-metallocorrole couple. C. Herrero, A. Quaranta, R. Ricoux, A. Trehoux, A. Mahammed, Z. Gross, F. Banse, J.-P. Mahy, Dalton Trans., 2016, 45, 706-710

Bio-inspired electron-delivering system for reductive activation of dioxygen at metal centres towards artificial flavoenzymes. Y. Roux, R. Ricoux, F. Avenier, J.-P. Mahy, Nature Communications, 2015, 6, 8509

An Artificial Enzyme Made by Covalent Grafting of an FeII Complex into β-Lactoglobulin: Molecular Chemistry, Oxidation Catalysis, and Reaction-Intermediate Monitoring in a Protein. C. Buron, K. Sénéchal-David, R. Ricoux, J.-P. Le Caër, V. Guérineau, P. Méjanelle, R. Guillot, C. Herrero, J.-P. Mahy, F. Banse, Chem. Eur. J., 2015, 21, 12188-12193

Synthesis and characterization of [Fe(BPMEN)ACC]SbF₆: a structural and functional mimic of ACC-oxidase. Y. Roux, W. Ghattas, F. Avenier, R. Guillot, A. J. Simaan, J.-P. Mahy, Dalton Trans., 2015, 44, 5966-5968

From "hemoabzymes" to "hemozymes": towards new biocatalysts for selective oxidations. J.-P. Mahy, J.-D. Maréchal, R. Ricoux, Chemical Communications, 2015, 51, 2476-2494

Catalytic oxidation of dibenzothiophene and thioanisole by a diiron(III) complex and hydrogen peroxide. A. Trehoux, Y. Roux, R. Guillot, J.-P. Mahy, F. Avenier, Journal of Molecular Catalysis A: Chemical, 2015, 396, 40-46

Various strategies for obtaining oxidative artificial hemoproteins with a catalytic oxidative activity: from "Hemoabzymes" to "Hemozymes"? J.-P. Mahy, J.-D. Maréchal, R. Ricoux, J. Porphyrins Phthalocyanines, 2014, 18, 1063-1092

Neocarzinostatin-based hybrid biocatalysts with a RNase like activity. A. Urvoas, W. Ghattas, J.-D. Maréchal, F. Avenier, F. Bellande, W. Mao, R. Ricoux, J.-P. Mahy, Bioorg. Med. Chem., 2014, 22, 5678-5686

Catalytic C-H Amination: A Reaction Now Accessible to Engineered Natural Enzymes. J.-P. Mahy, J. Ciesielski, P. Dauban, Angew. Chem. Intern. Ed., 2014, 53, 6862-6864

Neocarzinostatin-based hybrid biocatalysts for oxidation reactions. E. Sansiaume-Dagousset, A. Urvoas, K. Chelly, W. Ghattas, J.-D. Maréchal, J.-P. Mahy, R. Ricoux, Dalton Trans., 2014, 43, 8344-8354

A unique 1-amino-1-cyclopropane carboxylate cupric-cryptate hosting sodium. W. Ghattas, R. Ricoux, H. Korri-Youssoufi, R. Guillot, E. Riviere, J.-P. Mahy, Dalton Trans., 2014, 43, 7708-7711