Back to top

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

Career path
2016: CNRS director
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 Bio-inorganique 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.
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: Alessia Munzone (with C. Decroos, 2017-) & Rogelio Gomez Pineiro (with M. Orio, 2018-)

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

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

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)

Publications (54)
ReferenceGraphical Abstracts
Synthesis and Characterization of a Dinuclear Copper Complex Bearing a Hydrophobic Cavity as a Model for Copper-Containing Monooxygenases

A. Jalila Simaan, Olivier Schicke, Bruno Faure, Yannick Carissan, Michel Giorgi, Ariane Jalila Simaan, Marius Réglier, European Journal of Inorganic Chemistry, 2015, 2015, 3512-3518. <hal-02089409>
Gram-scale production of a basidiomycetous laccase in Aspergillus niger

Yasmina Mekmouche, Simeng Zhou, Angela M Cusano, Eric Record, Anne Lomascolo, Viviane Robert, A Jalila Simaan, Pierre Rousselot-Pailley, Sana Ullah, Florence Chaspoul, Thierry Tron, Journal of Bioscience and Bioengineering, 2014, 1-3. <hal-01268150>
Copper catalyzed oxidation of amino acids

Szabina Góger, József Pap, Dóra Bogáth, A. Jalila Simaan, Gabor Speier, Michel Giorgi, Jozsef Kaizer, Polyhedron, 2014, 73, 37-44. <hal-02091411>
Oxidative Degradation of Amino Acids and Aminophosphonic Acids by 2,2′-Bipyridine Complexes of Copper(II)

József Pap, Nadia El Bakkali-Tahéri, Antoine Fadel, Szabina Góger, Dóra Bogáth, Milán Molnár, Michel Giorgi, Gabor Speier, A. Jalila Simaan, Jozsef Kaizer, European Journal of Inorganic Chemistry, 2014, 2014, 2829-2838. <hal-02093862>
Visible Light-Driven O 2 Reduction by a Porphyrin–Laccase System

Theodore Lazarides, Igor Sazanovich, A. Jalila Simaan, Maria Kafentzi, Milan Delor, Yasmina Mekmouche, Bruno Faure, Julia Weinstein, Athanassios Coutsolelos, Thierry Tron, Maria Chrisanthi Kafentzi, Marius Réglier, Journal of the American Chemical Society, 2013, 135, 3095-3103. <hal-02091417>
Structural and Magnetic Characterization of a Tetranuclear Copper(II) Cubane Stabilized by Intramolecular Metal Cation−π Interactions

Raffaello Papadakis, Eric Riviere, Michel Giorgi, Hélène Jamet, Pierre Rousselot-Pailley, Marius Réglier, A. Jalila Simaan, Thierry Tron, Inorganic Chemistry, 2013, 52, 5824 - 5830. <hal-01653052>
Bio-inspired amino acid oxidation by a non-heme iron catalyst

Szabina Góger, Dóra Bogáth, Gábor Baráth, A. Jalila Simaan, Gabor Speier, Jozsef Kaizer, Journal of Inorganic Biochemistry, 2013, 123, 46-52. <hal-02091420>
Binuclear copper(II) complexes 1: Synthesis, characterization and evaluation of a new complex in phosphatase-like activity

Olivier Schicke, Bruno Faure, Michel Giorgi, A. Jalila Simaan, Marius Réglier, Inorganica Chimica Acta Reviews, 2012, 391, 189-194. <hal-02091433>
1-Aminocyclopropane-1-carboxylic acid oxidase: insight into cofactor binding from experimental and theoretical studies

Lydie Brisson, Nadia El Bakkali-Taheri, Michel Giorgi, Antoine Fadel, Jozsef Kaizer, Marius Réglier, Thierry Tron, El Hassan Ajandouz, A. Jalila Simaan, Journal of Biological Inorganic Chemistry, 2012, 17, 939–949. <hal-02091431>
Correlation between the SOD-Like Activity of Hexacoordinate Iron(II) Complexes and Their Fe3+/Fe2+ Redox Potentials

Balázs Kripli, Gábor Baráth, É. Balogh-Hergovich, Michel Giorgi, A. Jalila Simaan, László Párkányi, József S. Pap, József Kaizer, Gábor Speier Inorg. Chem. Commun. 2011, 14 (1), 205-209


Chapters of books (2)
ReferenceGraphical Abstracts
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⟩