Oral and poster presentation prizes awarded during the 2025 FrenchBIC Meeting

I am a second-year PhD student working in Christophe Léger’s group at BIP in Marseille. I started my studies in Italy at the University of Torino, where I concluded my Master studies with a thesis based on the development of an artificial redox chain for the regeneration of reduced NADH. During my Master I got in contact for the first time with the world of hydrogenases, which are amazing enzymes capable of catalysing the reversible conversion of protons and electrons into molecular hydrogen. This led me to my PhD in Marseille, where I’m currently working on the electrochemical characterization of atypical FeFe hydrogenases. In particular, I am interested on identifying which residues, located in the second coordination sphere around the active site, are capable of finely tuning the catalytic properties of these enzymes, allowing a huge diversification of responses even though they all share the same active site.

Tom Lacoma is a second year PhD student between Institut Parisien de Chimie Moléculaire (ChemBio) and Centre de Recherche Saint Antoine (TGF-β), under the supervision of Dr. Benoit Bertrand, Dr. Michèle Salmain and Pr. Joëlle Sobczak. His research focuses on the development of new anticancer gold (III) complexes displaying unusual reactivities, and their application to targeted therapy, with a particular focus on the reactivity and speciation of complexes in biologically relevant media. He presented his results on Biphenyl Gold(III) N-heterocyclic Carbenes (BGC) chelate complexes at FrenchBic2025, published very recently in ChemMedChem (DOI : 10.1002/cmdc.202500302).  This new family of 8 pairs of open neutral and chelated cationic complexes proved cytotoxic at micromolar levels, with a surprisingly mild impact of the structure on their activities. This was further rationalized by in depth speciation assays showing that all complexes react with chlorides in biological media and converge to their open neutral form. The neutral complexes are in turn able to induce mitochondrial depolarization, shortly followed by apoptotic cell death.

I am a postdoctoral researcher at the Laboratoire de Physique des 2 Infinis de Bordeaux (LP2IB), in the ICS-Neuro team, under the supervision of Richard Ortega.
My research focuses on autism spectrum disorders (ASD), which are the most common neurodevelopmental conditions in children. It is well established that metals—particularly lead—are associated with ASD.
Using synchrotron X-ray fluorescence (SXRF) and live-cell imaging on neurons, my research aims to investigate how lead affects zinc homeostasis and neuronal development in the context of ASD.

I’m a first-year PhD student in the labs of Yvain Nicolet and Sandrine Ollagnier at the IBS and LCBM in Grenoble. During my bachelor’s thesis in Bremen, Germany, I was first introduced to the fascinating world of metalloproteins. For my masters, I moved to Atlanta, Georgia to learn how to perform biomolecular simulations. This blend of experimental and computational experience allows me to tackle an old but no more fascinating project in the biotin synthase mechanism.

Biotin synthase catalyzes the final step in biotin biosynthesis, which inserts sulfur into the thiolane ring via radical chemistry. Until now, this has been assumed to consume the protein in a suicide reaction although previous in vivo studies have indicated a catalytic role of biotin synthase. Furthermore, a newly identified biotin synthase type preserves its auxiliary FeS cluster. With these discoveries in mind, the question of catalytic function and the mechanism of sulfur reinsertion arise. My project explores the mechanisms of both types through structural and biochemical studies, focusing on identifying sulfur transfer partners and characterizing reaction intermediates.