About one third of proteins are known to harbor a metal site, which is essential for their function. The metal ion can play various roles such as structuring the protein, transferring electrons or catalyzing hydrolytic or redox reactions.

Our team takes its inspiration from the metal sites of proteins and makes use of the properties of transition metal ions to design molecular catalysts for various reactions that are otherwise difficult to achieve. In particular, we are interested in the development of molecular catalysts bio-inspired from the hydrogenases metalloenzymes capable of H₂ evolution. These molecular catalysts are based on iron, an abundant and nontoxic metal, and are capable to perform dihydrogen auto-transfer reactions to access pharmaceutical active compounds in a sustainable manner.
Another research axis focuses on metallopeptides with two objectives: (i) to design and study models of zinc or iron sites of metalloproteins in order to understand their reactivity and (ii) to design probes for the detection of metal cations or biomolecules by luminescence or MRI. The research of the team relies on a strong expertise in various spectroscopies including electronic absorption, circular dichroism, luminescence and various magnetic spectroscopies (NMR, EPR, …). Moreover, the pmb team runs a Mössbauer platform dedicated to the study of iron-containing chemical and proteic systems.

Collaborations have been initiated with both French and international groups. The three research topics of the pmb team take benefit from external expertises, e.g. computational chemistry or cellular imaging and conversely several collaborations rely on our own expertise, for instance in Mössbauer spectroscopy.


Team members

Catalysis: