Researchers at the Humboldt-Universität zu Berlin and Charité – Universitätsmedizin Berlin have revealed the accurate structure of a hydrogen producing enzyme. This finding paves the way to the advancement of biotechnological methods for hydrogen production.
Some microbes such as algae and bacteria have enzymes that generate hydrogen. Using these hydrogen generating enzymes, dubbed as hydrogenases, researchers plan to generate hydrogen in artificial systems for the production of energy. However, oxygen permanently deactivates or even destroys most of the hydrogenases, thus restricting their biotechnological usage. Thus, hydrogenase that can continue its activity even in the existence of oxygen gains scientific interest.
The research team comprising Professor Spahn, who serves as the Director at Charité’s Institut für Physik und Biophysik, and Patrick Scheerer, who is the Head of the Working Group Proteinstrukturanalyse of the institute, has successfully demonstrated the three-dimensional structure of one such hydrogenase for the first time. The research team in partnership with researchers of the Humboldt-Universität zu Berlin, Dr. Oliver Lenz and Professor Bärbel Friedrich, have detected a unique iron-sulphur cluster in the center of the enzyme.
This iron-sulphur center performs like an electronic switch during the detoxification of harmful oxygen. This finding allows the researchers to corroborate the theory that certain hydrogenases can transform both oxygen and hydrogen in a catalytical method. Oxygen is reduced to harmless water during catalysis. Patrick Scheerer stated that these findings are critical to the development of biotechnological hydrogen-converting catalysts.
Source: http://www.charite.de