Institut de Chimie Moléculaire et des Matériaux d'Orsay

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

Antimicrobial Activity of Cationic Poly(3-hexylthiophene) Nanoparticles Coupled with Dual Fluorescent and Electrochemical Sensing: Theragnostic Prospect. N. Elgiddawy, S. Ren, W. Ghattas, W. M. A. E. Rouby, A. O. El-Gendy, A. A. Farghali, A. Yassar, H. Korri-Youssoufi, Sensors, 2021, 21, 1715

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

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

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

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

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

Crystal Structure of Phosphomannose Isomerase from Candida albicans Complexed with 5‐Phospho‐D‐Arabinonhydrazide. L. Ahmad, S. Plancqueel, V. Dubosclard, N. Lazar, W. Ghattas, I. Li De La Sierra‐gallay, H. Van Tilbeurgh, L. Salmon, FEBS Lett., 2018, 592, 1667-1680

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

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

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

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

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