New findings on hydrogen production
For the first time, scientists at Charité – Universitätsmedizin Berlin and Humboldt-Universität zu Berlin succeeded in unmasking the exact structure of a hydrogen generating enzyme. Therewith the authors deliver new findings on the development of biotechnological procedures for the production of hydrogen that can be used to generate and store energy. The results were now published online in the renowned Journal Nature*.
Molecular hydrogen is thought of as the energy carrier of the future and is already being tested as a promising renewable energy source, for example as fuel for vehicles. Certain microorganisms like bacteria and algae possess enzymes that release hydrogen. With the help of these hydrogen producing enzymes, the so called hydrogenases, scientists aim to produce hydrogen in artificial systems in order to generate energy. However, most of the hydrogenases are irreversibly inactivated or even destroyed by oxygen, which limits their biotechnological application. For this reason, hydrogenases that maintain their activity in the presence of oxygen are increasingly becoming the center of scientific interest. The research group of Prof. Spahn, director of the Institut für Physik und Biophysik of the Charité and Patrick Scheerer, head of the working group Proteinstrukturanalyse at the institute, succeeded for the first time in depicting the three-dimensional structure of such a hydrogenase. In cooperation with Prof. Bärbel Friedrich and Dr. Oliver Lenz from Humboldt-Universität zu Berlin they were able to identify a novel iron-sulphur cluster in the enzyme´s centre. This iron-sulphur centre acts as an electronic switch in the course of detoxification of detrimental oxygen. With this discovery, the scientists could substantiate the hypothesis that these particular hydrogenases are able to convert both hydrogen and oxygen in a catalytical manner. During catalysis, oxygen becomes reduced to harmless water.
“These discoveries can have great impact on the design of biotechnological hydrogen-converting catalysts”, says Patrick Scheerer. This is already the fifth study since 2008 that the Institut für Physik und Biophysik of the Charité publishes in “Nature”.
*Johannes Fritsch, Patrick Scheerer, Stefan Frielingsdorf, Sebastian Kroschinsky, Barbel Friedrich, Oliver Lenz, Christian M. T. Spahn: The crystal structure of an oxygen-tolerant hydrogenase uncovers a novel iron-sulphur centre. Nature, [epub ahead of print], doi: 10.1038/nature10505 (2011)
Link zum Institut für Physik und Biophysik: http://biophysik.charite.de/
Prof. Christian Spahn
Direktor des Instituts für Physik und Biophysik
Charité Campus Mitte
t: +49 30 450 524 131
Arbeitsgruppe Proteinstrukturanalyse des Instituts für Physik und Biophysik
t: +49 30 450 524 178
Charité Campus Mitte
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