A study recently published in the journal Nature Chemical Biology opens up new avenues in biohydrogen research, the Technical University of Berlin (TU Berlin) said on Friday.
Scientists at the TU Berlin succeeded in explaining the function of a molecular switch in biomolecules. The research was carried out together 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. This is because knowledge of the molecular structure of hydrogenases paves the way for the synthesis of chemical model compounds to product alternative energy source hydrogen, said TU Berlin.
Those 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.
"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," said microbiologist Dr. Oliver Lenz from the Institute of Chemistry of the TU Berlin.
The electronic switch is a key component of some proteins that are able to either produce hydrogen or to cleave hydrogen for energy.
Because of these properties, these biocatalysts called hydrogenases are the focus of research globally, said the study.