Société Française de Biochimie et Biologie Moléculaire



"Mechanism and dynamics of fatty acid photodecarboxylase"
Science (2021) 372; 6538. Sorigué, K. Hadjidemetriou, S. Blangy, G. Gotthard, A. Bonvalet, N. Coquelle, P. Samire, A. Aleksandrov, L. Antonucci, A. Benachir, S. Boutet, M. Byrdin, M. Cammarata, S. Carbajo, S. Cuiné, R. B. Doak, L. Foucar, A. Gorel, M. Grünbein, E. Hartmann, R. Hienerwadel, M. Hilpert, M. Kloos, T. J. Lane, B. Légeret, P. Legrand, Y. Li-Beisson, S. L. Y. Moulin, D. Nurizzo, G. Peltier, G. Schirò, R. L. Shoeman, M. Sliwa, X. Solinas, B. Zhuang, T. R. M. Barends, J.-P. Colletier, M. Joffre, A. Royant, C. Berthomieu, M. Weik, T. Domratcheva, K. Brettel, M. H. Vos, I. Schlichting, P. Arnoux, P. Müller, F. Beisson.


Damien Sorigué is 31 years old and studied at the Faculty of Science in Luminy (Aix Marseille University) where he obtained a Master's degree in Microbiology, Plant Biology and Biotechnology (MBVB). He completed his Master 2 his thesis and a post doctorate in the team Bioenergy and Microalgae (EBM) Cea Cadarache - BIAM. This team studies among others the metabolism of lipids in microalgae. Damien is now employ by CEA as young researcher and follows its investigation on the mechanism of Fatty acid photodecarboxylase (FAP) which converts fatty acids into hydrocarbons by using light energy (blue photons 400-530 nm). In the selected publication, Damien and his collaborators used a full range of techniques including static and time-resolved crystallography and spectroscopy, as well as biochemical and computational approaches to provide a detailed and comprehensive characterization of light-driven hydrocarbon formation by FAP. This enzyme, offers many biotechnological prospects, allowing the production of hydrocarbons in a biosourced way for chemistry, cosmetics or fuels. For basic research, photoenzymes are essential objects of study to understand the details of enzymatic mechanisms by ultrafast spectroscopy, or time-resolved crystallography (XFEL). An entertaining video presents the results obtained.


Damien Sorigué

BIAM EBM, CEA Cadarache 13115 Saint Paul lès Durance

This email address is being protected from spambots. You need JavaScript enabled to view it.

Summary of the article

Fatty acid photodecarboxylase (FAP) is a photoenzyme with potential green chemistry applications. By combining static, time-resolved, and cryotrapping spectroscopy and crystallography as well as computation, we characterized Chlorella variabilis FAP reaction intermediates on time scales from subpicoseconds to milliseconds. High-resolution crystal structures from synchrotron and free electron laser x-ray sources highlighted an unusual bent shape of the oxidized flavin chromophore. We demonstrate that decarboxylation occurs directly upon reduction of the excited flavin by the fatty acid substrate. Along with flavin reoxidation by the alkyl radical intermediate, a major fraction of the cleaved carbon dioxide unexpectedly transformed in 100 nanoseconds, most likely into bicarbonate. This reaction is orders of magnitude faster than in solution. Two strictly conserved residues, R451 and C432, are essential for substrate stabilization and functional charge transfer.