NEWS
7June 2021 ESRFnews
Project LEAPS to innovate A European open-science project that aims to help develop the next generation of photon sources and X-ray free-electron lasers in partnership with industry kicked off in April. LEAPS-INNOV is expected to enhance the long- term scientific competitiveness of European companies and research infrastructures, and foster the creation of new technological markets.
Established in 2017, LEAPS is a partnership of 16 light sources in Europe that aims to offer a common vision of using scientific excellence to solve global challenges, while boosting European competitiveness and integration. Although many of these light sources are already some of the best in the world, and many are awaiting major upgrades, new technologies will be needed to fully exploit them to meet the latest scientific and societal challenges. LEAPS-INNOV will identify and develop the key technologies that are crucial to future construction projects and upgrades, and prototype higher performance methodologies, protocols and instrumentation. The European Commission is providing 10 m of the funding, and the project partners a total of 8.3 m.
The overall goal of the project is to implement the LEAPS technical roadmap, by in particular exploring open-innovation strategies for partnership with European industry in the development of cutting-edge technologies to better supply LEAPS facilities and the general market, says Axel Kaprolat, who is responsible for the ESRF s overall participation.
The German synchrotron research centre DESY is co-ordinating the project overall and the ESRF will lead a work package in collaboration with the French synchrotron SOLEIL for the production of high-performance, extremely flat X-ray mirrors and grating substrates.
Circular economy enzyme comes to Gemini beamline An engineered enzyme that can quickly convert one-carbon atoms into a two-carbon compound has been evaluated at the ESRF s ID23-1 Gemini macromolecular crystallography beamline. The results bode well for the development of microbes that can convert carbon dioxide (CO2) in the atmosphere into carbon-based synthetics, thereby promoting a circular economy. The idea of a circular economy
is to re-purpose waste into valuable products, to minimise humanity s environmental footprint. The most pressing waste to tackle is CO2. This is already part of a natural carbon cycle involving cellular respiration and photosynthesis, but requires additional fixing due to anthropogenic emissions. One way to do this is with microbes that absorb CO2, a one-carbon molecule, and ultimately convert it into molecules containing more carbon atoms (multicarbons). These molecules can then be collected for the development of chemicals or synthetic intermediaries for use as fuels, pharmaceuticals and plastics. Such reactions exist naturally,
and typically involve multi-carbon acceptor molecules forming a bond with the single-carbon molecule; the new compounds are then rearranged and broken down again before they feed into the organism s central metabolism, while the original multi- carbon acceptor is regenerated. This is an energy-intensive process, and so scientists have been keen to develop a first step involving a bond between two one-carbon molecules. That would double the amount of carbon that is fixed per reaction, and also allow a faster entry into the central metabolism, says Maren Nattermann, the lead author of the latest research and a biochemist at the Max- Planck Institute for Terrestrial Microbiology in Marburg, Germany. This could make carbon fixation
quicker and less energy-demanding. Together with her colleagues
at the Max-Planck Institute, and the University of South Florida in Tampa, US, Nattermann identified a bacterial enzyme, MeOXC, that could albeit slowly convert a pair of one-carbon molecules into a two- carbon compound. The researchers then used a process known as directed evolution to iteratively engineer the enzyme into a variant with four mutations, MeOXC4, that worked 2000-fold faster. At the ID23-1 Gemini beamline, they evaluated the structures of the original enzyme and its final variant. By comparing the two, we could make inferences about how the structural changes within the enzyme had influenced its ability to catalyse our desired reaction, says Nattermann. Importantly, the researchers found that the variant also functioned in bacterial cells (ACS Catal. 11 5396). It would be great to see if bacterial
growth can be achieved on the basis of this new enzyme activity, Nattermann continues. This would constitute an important step towards a microbe that can turn CO2 into useful chemicals. For more on the circular economy,
see The green revolution , p19.
The overall structure of MeOXC, the enzyme targeted by directed evolution.