In Germany, a team from the Ruhr-Universität Bochum and the University of Oxford has found out how hydrogen-producing enzymes, or so-called hydrogenases, are activated during their biosynthesis. They showed how the cofactor – a part of the active center and at the same time the heart of the enzyme – is introduced into the interior.
Hydrogenases are biotechnologically interesting because they can produce hydrogen efficiently. “To optimize them for an industrial application, however, we must first understand the process of how the protein shell absorbs and activates the chemical cofactor,” says Prof. Dr. med. Thomas Happe.
The scientists studied the subgroup of so-called [FeFe] hydrogenases, which are the most efficient hydrogen producers. In nature, they occur in green algae. In their protein scaffold, the enzymes have an active center, the so-called H cluster, where the hydrogen is produced. It consists of two structural elements: a cluster of four iron and four sulfur atoms and the catalytic cofactor, consisting of two iron and two sulfur atoms. “This cofactor is the linchpin of the enzyme,” explains Oliver Lampret.