Thus, they provide new insights into the development of biotechnological processes for the production of hydrogen, which can lead to environmentally friendly energy production and storage. The results of the work were published online in the prestigious journal Nature.
Hydrogen is an energy carrier of the future as an alternative energy source which can be used for various purposes such as a fuel for motor vehicles, already in the testing. Certain microorganisms such as algae and bacteria have enzymes that enable them to liberate hydrogen itself. Researchers aim to use this hydrogen-forming enzymes, called hydrogenases, in artificial systems to produce hydrogen to gain energy from it in future. Most hydrogenases are inactivated by oxygen, however, or even destroyed, making these enzymes for biotechnological application only limited applicability. For this reason, move the few hydrogenases that can work well in an oxygen rich environment, the focus of scientific interest.
The research group of Prof. Spahn, director of the Institute of Physics and Biophysics, Charité Scheerer and Patrick Head, the working group was protein structure analysis at the Institute, representing the first detailed three-dimensional structure of such a hydrogenase. In cooperation with Prof. Dr. Bärbel Friedrich and Oliver Lenz, Humboldt University was able to identify a currently unique iron-sulfur compound in the center of the enzyme. This iron-sulfur center allows the hydrogenase to produce hydrogen and the other one to the unwanted oxygen put into harmless water.