Newsportal - Ruhr-Universität Bochum

Certain enzymes, such as hydrogen-producing hydrogenases, are unstable in the presence of oxygen. Researchers at RUB have identified the reasons on the atomic level. Using x-ray structure analysis, they showed that certain iron atoms in the core of the enzyme are altered in the presence of oxygen, gradually leading to the disintegration of the entire active centre. The team outlines the results in the Journal of the American Chemical Society (JACS), published online on 14 October 2019.

Since Julian Esselborn is working at the University of California, the Bochum researchers Eckhard Hofmann (left ) und Thomas Happe (right) exchange information with him via video chat.

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The experiments were carried out jointly by three RUB groups: the photobiotechnology research group was represented by Dr. Julian Esselborn – today at the University of California, San Diego –, Professor Thomas Happe and Dr. Leonie Kertess. The team collaborated with Professor Eckhard Hofmann from the Protein Crystallography Group and Dr. Ulf-Peter Apfel from the Chair of Inorganic Chemistry I.