A team of scientists, including many in the Molecular Biophysics and Integrated Bioimaging Division, uncovered new details about the reaction that powers photosynthesis. Understanding this reaction could lead to world-changing advances in technology, medicine, or energy––and also gives insight into how the enzyme photosystem II produces the oxygen we breathe. Their latest work was recently published in Nature Communications and two of the authors, Vittal Yachandra and Philipp Simon, spoke with Strategic Communications about that, shooting stuff with lasers, and why they chose this field of research.
As part of an international collaboration, researchers at Lawrence Berkeley National Laboratory (Berkeley Lab), the Diamond Light Source synchrotron facility, and Oxford and Bristol Universities in England have developed a novel sample delivery system that expands the limited toolkit for performing dynamic structural biology studies of enzyme catalysis, which have so far mostly been limited to a small number of light-driven enzymes.
Scientists have determined the structure of a unique enzyme, produced by a species of methane-eating bacteria, that converts the greenhouse gas into methanol – a highly versatile liquid fuel and industrial product ingredient.
Their new study, published in the Journal of the American Chemical Society, is the first to report the structure of the enzyme, called soluble methane monooxygenase (sMMO), at room temperature in both its reduced and oxidized forms. This detailed structural information will help researchers design efficient catalysts for industrial methane to methanol conversion processes.
An international team led by researchers in Berkeley Lab’s Molecular Biophysics and Integrated Bioimaging (MBIB) Division has revealed a key step in the molecular mechanism behind the water splitting reaction of photosynthesis. The finding could help inform the design of renewable energy technology.
An article published in the Computing Sciences News Center describes how Biosciences researchers are using a superfacility framework of experimental instrumentation with computational and data facilities to unravel the long-standing mystery of how Photosystem (PSII) works. The protein complex plays a crucial role in photosynthesis, making it key to achieving artificial photosynthesis that could produce fuels using sunlight and carbon dioxide. Researchers—led by Vittal Yachandra, Junko Yano, and Jan Kern in Molecular Biophysics and Integrated Bioimaging (MBIB)—recently began using ESnet to enable real-time processing of experimental data collected at the SLAC National Accelerator Laboratory’s Linac Coherent Light Source (LCLS) at NERSC to observe this water-splitting protein in action. Asmit Bhowmick, a postdoctoral researcher in the laboratory of MBIB senior scientist Nicholas Sauter, is quoted in the article.