Oral presentation prizes to Philipp Gotico and Livia Meszaros, during the FrenchBIC 2017 summer school
Philipp Gotico got his MS degree in Chemistry under the Erasmus Mundus Surface, Electro-, Radio-, and Photo-Chemistry (SERP-Chem) Program in 2016 obtaining three diplomas from University of Genova (Italy), University of Porto (Portugal), and University of Paris Saclay (France).
He is now a PhD student in CEA Saclay funded under the IRTELIS program. He works in a collaborative group between Winfried Leibl of Laboratoire des Mécanismes fondamentaux de la Bioénergétique (LMB) in the Institut de Biologie et de Technologies de Saclay (IBITECS) in CEA Saclay and Ally Aukauloo of Laboratoire de Chimie Inorganique (LCI) in the Institut de Chimie Moléculaire et des Matériaux d'Orsay (ICMMO) in Université Paris Saclay.
He presented his initial insights in the French BIC summer school entitled “In the Realm of Artificial Photosynthesis: Development of Photocatalysts for CO2 Reduction” after investigating a ruthenium-rhenium dyad as a photocatalyst sytem. From these insights, he is now developing a novel catalyst with some bio-inspiration from CO dehydrogenase, known to be effective in the reversible reduction of CO2 to CO.
Livia S. Meszaros is researcher in the Biophysics and Bioinorganic Chemistry group at Uppsala University, Department of Chemistry, Sweden. Her main interest is the mechanism and structure of metalloenzymes in particular mimicking of the natural enzymes with synthetic chemical methods.
The title of her presented work was: Synthetic biology meets Synthetic chemistry - In vivo activation of an apo-hydrogenase using synthetic complexes. [FeFe] hydrogenases catalyze the reduction of protons, and oxidation of hydrogen gas, with remarkable efficiency. The reaction occurs at the H-cluster, which contains an organometallic [2Fe] subsite. The unique nature of the [2Fe] subsite makes it dependent on a specific set of maturation enzymes for its biosynthesis and incorporation into the apo-enzyme. In her presentation she reported on how the natural maturation system can be circumvented, and the apo-enzyme activated in vivo by synthetic active site analogues taken up by the living cell. The presented method provides new perspectives for examination of hydrogenase enzymes.
Reference: Khanna N, Esmieu C, Mészáros LS, Lindblad P, Berggren G. (2017) In vivo activation of an [FeFe] hydrogenase using synthetic cofactors. Energy and Environ. Sci. 10: 1563 – 1567.