Department of Biochemistry and Biophysics

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  • Researchers at DBB explore the functional dynamics of an ancient membrane-bound hydrogenase 2021-12-01 Biological energy conversion is based on membrane-bound proteins that convert chemical or light energy into an electro-chemical gradient across a biological membrane. The primordial archaea convert energy by membrane-bound hydrogenases (Mbh) that produce hydrogen gas (H2) and couples this to proton pumping and Na+/H+ exchange across the archaeal membranes. However, the molecular principles of its redox-driven ion-transport mechanism remain puzzling and of major interest for understanding bioenergetic principles of early cells.
  • Christian Broberger awarded council professorship by the Swedish Research Council 2021-11-25 The Swedish Research Council has decided on council professorships in medicine and health. Of the three new professorships, one is awarded to Stockholm University.
  • Researchers granted funding from the Swedish Cancer Society 2021-11-25 Six researchers at Stockholm University including David Drew, Einar Hallberg and Mats Nilsson at DBB are granted grants corresponding to a total of SEK 18.6 million from the Swedish Cancer Society.
  • First high-resolution structure of neurofibromine paves the way for cancer research 2021-11-03 Three researchers at Stockholm University and SciLifeLab, together with a researcher at the Institute of Genetic Epidemiology in Innsbruck, have developed the first high-resolution structure of the human protein and tumor inhibitor neurofibromine, using cryo-electron microscopy. The study was recently published in the journal Nature and provides a greater knowledge of how neurofibromine works.
  • Press release: Gunnar von Heijne awarded the Celcius medal by the Swedish Society of Science 2021-11-01 At the Royal Swedish Society of Science's anniversary on the 30th of October at Uppsala Castle, the Celsius medal in gold was awarded to Professor Gunnar von Heijne, Department of Biochemistry and Biophysics at Stockholm University.
  • Structure of the native pyruvate dehydrogenase complex reveals the mechanism of substrate insertion 2021-09-08 The pyruvate dehydrogenase complex is a multienzyme complex of megadalton size that converts pyruvate into acetyl-coenzyme A, thereby linking glycolysis to the citric acid cycle and to the biosynthesis of fatty acids. In a new study from DBB, scientists for the first time, reveal how the lipoyl domains interact with the core of a pyruvate dehydrogenase complex, to insert substrate into the active site. The study is published in Nature Communications.