Scientists at the TU Berlin succeeded in explaining the function of a molecular switch in biomolecules. The research was carried out with the Free University Berlin, the Charite and the Humboldt University of Berlin.

　　The findings are significant not only for basic research but also for the technical application of biological hydrogen conversion, scientists said.

　　Knowledge of the molecular structure of hydrogenases paves the way for the synthesis of chemical model compounds to produce hydrogen, regarded as an alternative energy source, said TU Berlin.

　　German <a href=http://www.hxen.com target=_blank class=infotextkey>study</a> opens up new avenues in biohydrogen research

　　These biocatalysts called hydrogenases, which are not inactivated by the oxygen in the air, are of particular interest of the researchers. Due to their unusual property of oxygen compatibility, the molecular switch plays a key role.

　　The switch refers to a cluster of iron and sulfur atoms, which can conduct or optionally store electrons.

　　Understanding the catalytic mechanism of hydrogenase might help scientists design clean biological energy sources, such as algae, that produce hydrogen.

　　"Because of its transdisciplinary methodology, our research group could decipher how the electronic switch allows the hydrogenase to detoxify the harmful oxygen, while ensuring that further energy is obtained from hydrogen," says microbiologist Dr. Oliver Lenz from the Institute of Chemistry of the TU Berlin.

　　As the electronic switch is a key component of some proteins that are able to either produce hydrogen or to split hydrogen for energy, hydrogenases are the focus of research globally, said the study.

　　Hydrogen may be obtained from fossil sources, but these sources are unsustainable. So an important future application of hydrogen could be as an alternative for fossil fuels once global oil deposits are depleted.