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A. Jalila

Dr. A. jalila Simaan's picture
A. Jalila
AMU iSm2 Service 342
Campus Scientifique de St Jérôme
Marseille cedex 20
Phone number
0491 28 84 40
Date of entry
Career path

2016: CNRS director (Marseille)

2002: CNRS researcher in Marseille

2000-2001 : Postdoc in Raman Spectroscopy with Prof. Peter Hildebrandt/ Max Planck Institut für Strahlenchemie, Mülheim / Ruhr (Allemagne) et à Instituto de Tecnológia Química e Biológica, Oeiras (Portugal)

1997-2000 : PhD in Bioinirganic chemistry, Paris-Sud University (Orsay) / Prof Jean-Jacques GIRERD and Frédéric Banse

1996 : «Agrégation externe de Sciences Physiques Option Chimie ».

1993 -1997: Student at the « Ecole Normale Supérieure de Cachan »  Chemistry department. Physical Chemistry studies at Université Paris-Sud, Orsay.

  • Ecole Normale Supérieure de Cachan scolarship (1993-1997)
  • PhD grant from French Ministry (1997-2000)
  • City of Marseille grant (2002)
  • Invited researcher at the university of Cuernavaca (UNAM), Mexico (2010)
  • City of Marseille attractivity trophee (2017)
  • Biomimetic Innovation Price -Region PACA (2019)
Research themes

Copper containing Monooxygenases enzymes and model complexes

In collaboration with Marius Réglier, Christophe Decroos, Bruno Faure, Maylis Orio (iSm2/BiosCiences)
Current PhD students: , Manon Pujol (with C. Decroos; 2019-); Stefani Gamboa (with M. Orio; 2019-); Yongxing Wang (with A. Martinez, 2021-); Rébecca Leblay (with B. faure, 2021-);
Former students: Alessia Munzone (with C. Decroos, 2017-2021),  Rogelio Gomez Pineiro (with M. Orio, 2018-2021)

Copper containing Monooxygenases couple dioxygen reductive activation to oxygen atom transfer into a substrate's C-H bond. Copper Monooxygenases display active sites of diverse nuclearities and structures. We are interested in several monooxygenases and in particular, in Lytic Polysaccharide Monooxygenases or LPMOs, mononuclear copper-containing enzymes that boost recalcitrant polysaccharide degradation (biomass) via oxidative pathways. LPMO possess a rare coordination motif: the N-terminal histidine is bound to the copper ion via both its imidazole ring and the amino terminal group (Histidine-brace motif).

Our studies are centered on  :

  • Understanding the mechanism of enzymatic systems (e.g. LPMOs)
  • Preparing copper-containing bio-inspired models and trapping reaction intermediates
  • Performing water oxidation/activation with copper complexes
  • preparing bioinspired catalysts for improved biomass utilization

External collaborations: Dr. Catherine Belle, Dr. Hélène Jamet and Dr. Aurore Thibon-Pourret (Université Grenoble-Alpes / CNRS); Dr. Nicolas Le Poul (Université de Bretagne Occidentale, CNRS); Prof. Ivan Castillo (UNAM, Mexico, ECOS-Nord project);

ACC Oxidase, a non-heme iron(II) enzyme

PhD student (past): Dr. Eugénie Fournier (with Prof. V. Belle, 2015-2018)

The plant hormone ethylene is essential for many aspects of plant life germination, senescence, fruit ripening and defense mechanisms. Ethylene is directly biosynthesized from 1-aminocyclopropane carboxylic acid (ACC), a metabolite of methionine. This step is catalyzed by ACC Oxidase a non-heme iron(II) containing enzyme. The conversion of ACC into ethylene requires the presence of ferrous ions, dioxygen and ascorbate. In addition, ACCO also requires the presence of CO2 (or HCO3-) for activity.

The crystallographic structures revealed a coeur folded in beta barrel that contains the active site. The iron(II)  ion is coordinated by the side chains of 2 histidines and one aspartate in a classical facial triad. Although several set of structures have been obtained, there are still question on the active conformation of the enzyme and in particular, that of the C-terminal part (in red on the figure ).Thanks to an interdisciplinary approach we aim at getting more information on this enzyme 

Our studies are centered on:

  • Understanding the mode of action of the enzyme
  • Exploring metal / activity modification
  • Getting information on the active conformation and dynamic of the C-terminal part
  • preparing model complexes
  • using ACCO as a platform to develop artificial enzymes

External collaborations: Prof. Valérie Belle and Dr. Marlène Martinho (Université d'Aix-Marseille); Prof. Christian Limberg (Humboldt University, Berlin, Germany); Prof. József Kaizer (University of Pannonia, Veszprém, Hungary); Dr. Wadih Ghattas & Prof. Jean-Pierre Mahy (Université Paris-Saclay); Prof. Sam De Visser (Univ. Manchester, UK).

Collaborations and groups

French groups

  • Dr. Wadih Ghattas & Prof. Jean-Pierre Mahy (Université Paris-Saclay)
  • Prof. Valérie Belle et Dr. Marlène Martinho (Université d'Aix-Marseille)
  • Dr. Catherine Belle, Dr. Hélène Jamet and Dr. Aurore Thibon-Pourret (Université Grenoble-Alpes / CNRS)
  • Dr. Nicolas Le Poul (Université de Bretagne Occidentale, CNRS);

International groups

  • Prof. Christian Limberg (Humboldt University, Berlin, Germany)
  • Prof. Kallol Ray (Humboldt University, Berlin, Germany)
  • Prof. József Kaizer (University of Pannonia, Veszprém, Hungary)
  • Prof. Sam de Visser (Univ. Manchester, UK).
  •  Prof. Ivan Castillo (UNAM, Mexico, ECOS-Nord project)
Administrative responsabilities

Responsabilités en cours

Scientific outreach efforts

Diels-Alderases artificielles au service de la chimie verte. Wadih Ghattas, Jean-Pierre Mahy, Rémy Ricoux, A. Jalila Simaan, Marius Réglier

Techniques de l’Ingénieur, date publication le 10 septembre 2021, ref : IN404 V1

Publications (73)
Reference Graphical abstract HAL

Integrated Experimental and Theoretical Investigation of Copper Active Site Properties of a Lytic Polysaccharide Monooxygenase from Serratia marcescens

Alessia Munzone, Manon Pujol, Ashish Tamhankar, Chris Joseph, Ievgen Mazurenko, Marius Réglier, Sergio Jannuzzi, Antoine Royant, Giuseppe Sicoli, Serena Debeer, Maylis Orio, A. Jalila Simaan, Christophe Decroos, Inorganic Chemistry, 2024, Online ahead of print. <hal-04595887>

Light-Induced Reactivity Switch at O2–Activating Bioinspired Copper(I) Complexes

Donglin Diao, Anna Baidiuk, Leo Chaussy, Iago de Assis Modenez, Xavi Ribas, Marius Réglier, Vlad Martin-Diaconescu, Paola Nava, A. Jalila Simaan, Alexandre Martinez, Cédric Colomban, JACS Au, 2024. <hal-04564103>

LPMO‐like activity of bioinspired copper complexes: from model substrate to extended polysaccharides

Rébecca Leblay, Rafael Delgadillo-Ruiz, Christophe Decroos, Christelle Hureau, Marius Réglier, Ivan Castillo Pérez, Bruno Faure, A. Jalila Simaan, ChemCatChem, 2023, 15, e202300933. <hal-04231361>

Controlled Immobilization of a Palladium Complex/Laccase Hybrid into a Macrocellular Siliceous Host

Fangfang Yang, Pierre Rousselot-Pailley, Cendrine Nicoletti, A. Jalila Simaan, Bruno Faure, Elise Courvoisier-Dezord, Agnès Amouric, Yolande Charmasson, Rénal Backov, Thierry Tron, Yasmina Mekmouche, ChemPlusChem, 2023, 88, e202300156. <hal-04105029>

Bioinspired complexes confined in well-defined capsules: getting closer to metalloenzyme functionalities

Donglin Diao, A. Jalila Simaan, Alexandre Martinez, Cédric Colomban, Chemical Communications, 2023. <hal-04047768>

Tandem metalloenzymes gate plant cell entry by pathogenic fungi

Bastien Bissaro, Sayo Kodama, Takumi Nishiuchi, Anna Maria Díaz-Rovira, Hayat Hage, David Ribeaucourt, Mireille Haon, Sacha Grisel, A. Jalila Simaan, Fred Beisson, Stephanie Forget, Harry Brumer, Marie-Noëlle Rosso, Victor Guallar, Richard O'Connell, Mickaël Lafond, Yasuyuki Kubo, Jean‐guy Berrin, Science Advances, 2022, 8. <hal-03918339>

Cell-penetrating peptide-conjugated copper complexes for redox-mediated anticancer therapy

Quim Peña, Sergi Rodríguez-Calado, A. Jalila Simaan, Mercè Capdevila, Pau Bayón, Oscar Palacios, Julia Lorenzo, Olga Iranzo, Frontiers in Pharmacology, 2022, 13. <hal-03881444>

Photocatalytic generation of a non-heme Fe(III)-hydroperoxo species with O$_2$ in water for oxygen atom transfer reaction

Eva Pugliese, Nhat Tam Vo, Alain Boussac, Frédéric Banse, Yasmina Mekmouche, A. Jalila Simaan, Thierry Tron, Philipp Gotico, Marie Sircoglou, Zakaria Halime, Winfried Leibl, Ally Aukauloo, Chemical Science, 2022, 2012. <hal-03795563>

Computational Insights of Selective Intramolecular O‐atom Transfer Mediated by Bioinspired Copper Complexes

Stefani Gamboa-Ramírez, Bruno Faure, M. Réglier, A. Jalila Simaan, Maylis Orio, Chemistry - A European Journal, 2022, e202202206. <hal-03789397>

A caged tris(2-pyridylmethyl)amine ligand equipped with a C triazole –H hydrogen bonding cavity

Gege Qiu, Donglin Diao, Leo Chaussy, Sabine Michaud-Chevallier, A. Jalila Simaan, Paola Nava, Alexandre Martinez, Cédric Colomban, Dalton Transactions, 2022, 51, 10702-10706. <hal-03789423>


Chapters of books (3)
Reference Graphical abstract HAL

Clarisse Faure, Amaury Du Moulinet D’hardemare, Hélène Jamet, Catherine Belle, Elisabetta Bergantino, et al.. Transition State Analogue Molecules as Mechanistic Tools and Inhibitors for Tyrosinase. Copper Bioinorganic Chemistry, WORLD SCIENTIFIC, pp.45-80, 2023, ⟨10.1142/9789811269493_0002⟩. ⟨hal-04186414⟩

A. Jalila Simaan, Alda Lisa Concia, Alessia Munzone, Maria-Chrysanthi Kafentzi, Amélie Kochem, et al.. Modeling the Mononuclear Copper Monooxygenase Active Site. Series on Chemistry, Energy and the Environment: Volume 5 Bioinspired Chemistry; From Enzymes to Synthetic Models, pp.185-263, 2019, ⟨10.1142/9789813274440_0008⟩. ⟨hal-02094996⟩

A. Jalila Simaan, Marius Réglier. CHAPTER 20. 1-Aminocyclopropane-1-Carboxylic Acid Oxidase. 2-oxoglutarate-dependent oxygenases RSC Metallobiology Series, 3., pp.425-437, 2015, ⟨10.1039/9781782621959-00425⟩. ⟨hal-02095042⟩