The marine bacterium Alcanivorax borkumensis feeds on oil, multiplying rapidly in the wake of oil spills, and thereby accelerating the elimination of the pollution, in many cases. It does this by producing an “organic dishwashing liquid” which it uses to attach itself to oil droplets. Researchers from the University of Bonn, RWTH Aachen University, Heinrich Heine University Düsseldorf and research center Forschungszentrum Jülich have now discovered the mechanism by which this “organic dishwashing liquid” is synthesized. Published in the prominent international journal Nature Chemical Biology, the research findings could allow the breeding of more efficient strains of oil-degrading bacteria.

In the absence of air, microorganisms produce hydrogen using an enzyme called [FeFe]-hydrogenase, one of the most efficient hydrogen-producing biocatalysts known and a promising tool for green hydrogen energy. However, these enzymes are rapidly destroyed when exposed to air, which has so far limited their industrial use. Joint efforts led by scientists from the Photobiotechnology group and the Center for Theoretical Chemistry at Ruhr University Bochum, Germany, isolated a new type of oxygen-stable [FeFe]-hydrogenase and revealed its “tricks” for this oxygen-stability. The results are published in “Journal of American Chemical Society” on April 23, 2025.

This study reports two cryo-EM structures of the Nipah virus (NiV) polymerase L-P complex in its full-length and truncated forms. These structures elucidate the RNA-dependent RNA polymerase (RdRp) and polyribonucleotidyl transferase (PRNTase) domains of the L protein, as well as the tetrameric P protein bundle bound to the L-RdRp. This work establishes a foundational framework for understanding the NiV polymerase mechanism and provides critical insights for the rational design of antiviral therapeutics targeting the polymerase complex  

In a new study, researchers at the University of Würzburg are investigating the interaction of major global change drivers on insects.

In neurodegenerative diseases such as Alzheimer's or Parkinson's, proteins accumulate in the body's cells, fold incorrectly and clump together to form larger aggregates. Normally, cells are able to remove these aggregates themselves. However, if a certain enzyme is blocked, this clean-up process no longer works. This is shown in a new study by an international research team led by the University of Würzburg. The new findings provide a better understanding of the molecular basis of these processes.

The North Korean government engages in unsustainable and illegal wildlife trade, which includes species protected under its own laws and poses a threat to biodiversity recovery in the region, finds a groundbreaking new study by UCL researchers.