To carry out their activities, Research Teams of the Frédéric Joliot Institute for Life Sciences have developed high-profile technological platforms in many areas : biomedical imaging, structural biology, metabolomics, High-Throughput screening, level 3 microbiological safety laboratory...
Within the Institute, the "Funding Research and Technology Transfer" team is at your disposal to identify the scientists and the skills you need to set up a joint project, to define the terms of a collaboration contract or study.
Whether you are an academic, a SME or an industrialist, our team informs and advices you about the possibilities of consortium assembly, technology transfer, patent licensing or use of our platforms.
The team is also at the disposal of the researchers of the institute to accompany them in achieving their valorization objectives.
Scientific result | Biotechnology | Bioenergy | Photosynthesis
Researchers at BIAM and I2BC@Saclay, in collaboration with Japanese colleagues from Okayama University and Ehime, have characterized in a cyanobacterium a minor protein that diverts part of the energy from photosynthesis to secondary metabolic pathways. This discovery is promising to exploit these metabolic pathways in a biotechnological process of bioenergy production.
Photosynthetic [2Fe-2S] plant-type ferredoxins have a central role in electron transfer between the photosynthetic chain and various metabolic pathways. Several genes are coding for [2Fe-2S] ferredoxins in cyanobacteria, with four in the thermophilic cyanobacterium Thermosynechococcus elongatus. The structure and functional properties of the major ferredoxin Fd1 are well known but data on the other ferredoxins are scarce. We report the structural and functional properties of a novel minor type ferredoxin, Fd2 of T. elongatus, homologous to Fed4 from Synechocystis sp. PCC 6803. Remarkably, the midpoint potential of Fd2, Em = −440 mV, is lower than that of Fd1, Em = −372 mV. However, while Fd2 can efficiently react with photosystem I or nitrite reductase, time-resolved spectroscopy shows that Fd2 has a very low capacity to reduce ferredoxin-NADP+ oxidoreductase (FNR). These unique Fd2 properties are discussed in relation with its structure, solved at 1.38 Å resolution. The Fd2 structure significantly differs from other known ferredoxins structures in loop 2, N-terminal region, hydrogen bonding networks and surface charge distributions. UV–Vis, EPR, and Mid- and Far-IR data also show that the electronic properties of the [2Fe-2S] cluster of Fd2 and its interaction with the protein differ from those of Fd1 both in the oxidized and reduced states. The structural analysis allows to propose that valine in the motif Cys53ValAsnCys56 of Fd2 and the specific orientation of Phe72, explain the electron transfer properties of Fd2. Strikingly, the nature of these residues correlates with different phylogenetic groups of cyanobacterial Fds. With its low redox potential and its discrimination against FNR, Fd2 exhibits a unique capacity to direct efficiently photosynthetic electrons to metabolic pathways not dependent on FNR.
T. Motomura, L. Zuccarello, P. Sétif, et al. , An alternative plant-like cyanobacterial ferredoxin with unprecedented structural and functional properties: Ferredoxin with low Em discriminating against FNR, BBA Bioenergetics (2019), Sous presse. https://doi.org/10.1016/j.bbabio.2019.148084
CEA is a French government-funded technological research organisation in four main areas: low-carbon energies, defense and security, information technologies and health technologies. A prominent player in the European Research Area, it is involved in setting up collaborative projects with many partners around the world.