Scientists from the Faculty of Biology and Biotechnology at the RUB have published a report in the Journal of Biological Chemistry explaining why enzymes used for the production of hydrogen are so sensitive to oxygen. In collaboration with researchers from Berlin, they used spectroscopic methods to investigate the time course of the processes that lead to the inactivation of the enzyme's iron center. "Such enzymes, the so-called hydrogenases, could be extremely significant for the production of hydrogen with the help of biological or chemical catalysts", explains Camilla Lambertz from the RUB study group for photobiotechnology. "Their extreme sensitivity to oxygen is however a major problem. In future, our results could help to develop enzymes that are more robust."
Oxygen as a friend and as an enemy
Oxygen is crucial for the survival of most animals and plants. It is however toxic for many living creatures if the concentration thereof is too high, and some organisms can even only exist entirely without oxygen. Sensitivity to oxygen is also present at the protein level. A large number of enzymes, for example, hydrogenases are known to be irreversibly destroyed by oxygen. Hydrogenases are biological catalysts that convert protons and electrons into technically usable hydrogen. The RUB team of Prof. Thomas Happe is doing research on so-called [FeFe]-hydrogenases which are capable of producing particularly large amounts of hydrogen. The generation of hydrogen takes place at the H-cluster, consisting of a di-iron and four-iron subcluster which, together with other ligands, form the reactive center.
Oxygen attacks the iron centers
The researchers, working in collaboration with Dr. Michael Haumann's team in Berlin, discovered that oxygen binds to the di-iron center of the hydrogenase, which initiates the inactivation of another part of the enzyme consisting of four further iron atoms. In this project, sponso
|Contact: Camilla Lambertz|