A team from Ruhr-Universität Bochum and the University of Oxford has discovered how hydrogen-producing enzymes, called hydrogenases, are activated during their biosynthesis.
A team from Ruhr-Universität Bochum and the University of Oxford has discovered how hydrogen-producing enzymes, called hydrogenases, are activated during their biosynthesis. They showed how the cofactor – part of the active centre and also the heart of the enzyme – is introduced inside.
Hydrogenases are of biotechnological interest as they are able to efficiently produce hydrogen. “In order to optimise them for an industrial application, we first need to understand the process of how the protein shell takes up and activates the chemical cofactor,” says Professor Thomas Happe. A team led by Oliver Lampret and Thomas Happe from the Bochum-based Photobiotechnology Research Group published the results in the journal “Proceedings of the National Academy of Sciences”, PNAS for short, on 23 July 2019.
The researchers investigated the subgroup of [FeFe]-hydrogenases, which are the most efficient hydrogen producers. In nature, they can be found in green algae. Within their protein scaffold, the enzymes have an active centre, the so-called H-cluster, where the hydrogen is produced. It is comprised of two structural elements: a cluster containing four iron and four sulphur atoms, and the catalytic cofactor, which consists of two iron and two sulphur atoms. “This cofactor is the linchpin of the enzyme,” explains Oliver Lampret.
Read more at Ruhr-Universität Bochum (RUB)
Image: Thomas Happe (left) and Oliver Lampret aim at understanding the workings of hydrogen producing enzymes in detail. CREDIT: RUB, Kramer
