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Hydrogenases are very sensitive to oxygen. Thus, experiments with the enzymes have to take place in a sealed environment. © RUB, Marquard
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. © Privat

How oxygen destroys the core of important enzymes

JACS: New findings are expected to help protect the hydrogen-producing enzymes from harmful oxygen - which is interesting for biotechnological applications.

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.

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.

 

Additional Information

Detailed Press Release

Original Publication: Julian Esselborn, Leonie Kertess, Ulf-Peter Apfel, Eckhard Hofmann, Thomas Happe: Loss of specific active-site iron atoms in oxygen exposed [Fe-Fe]-hydrogenase determined by detailed X-ray structure analyses, in: Journal of the American Chemical Society, 2019, DOI: 10.1021/jacs.9b07808

 

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Wie Sauerstoff das Herzstück wichtiger Enzyme zerstört

 

Neue Erkenntnisse sollen helfen, Wasserstoff produzierende Enzyme künftig vor schädlichen Sauerstoff zu schützen – interessant für die Biotechnologie.

Bestimmte Enzyme, wie die Wasserstoff produzierende Hydrogenasen, sind in Anwesenheit von Sauerstoff instabil. Woran das liegt, haben RUB-Forscherinnen und -Forscher auf atomarer Eben aufgeklärt. Mithilfe der Röntgenstrukturanalyse zeigten sie, wie sich bestimmte Eisenatome im Zentrum des Enzyms in Anwesenheit von Sauerstoff verändern, was nach und nach zum Zerfall des gesamten Zentrums führt. Die Ergebnisse berichten sie im Journal of the American Chemical Society, kurz JACS, online veröffentlicht am 14. Oktober 2019.

Für die Experimente arbeiteten drei Gruppen der RUB zusammen: Aus der Arbeitsgruppe Photobiotechnologie waren Dr. Julian Esselborn – heute an der University of California, San Diego –, Prof. Dr. Thomas Happe und Dr. Leonie Kertess beteiligt. Das Team kooperierte mit Prof. Dr. Eckhard Hofmann aus der Arbeitsgruppe Röntgenstrukturanalyse an Proteinen und Dr. Ulf-Peter Apfel vom Lehrstuhl Anorganische Chemie I.

 

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Ausführliche Presseinformation

Originalveröffentlichung: Julian Esselborn, Leonie Kertess, Ulf-Peter Apfel, Eckhard Hofmann, Thomas Happe: Loss of specific active-site iron atoms in oxygen exposed [Fe-Fe]-hydrogenase determined by detailed X-ray structure analyses, in: Journal of the American Chemical Society, 2019, DOI: 10.1021/jacs.9b07808

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