Enzymes perform very specific functions and require little energy which is why biocatalysts are also of interest to the chemical industry. The study was published in the journal Nature Reviews Chemistry.
Professor Thomas Happe and Associate Professor Anja Hemschemeier from the Photobiotechnology workgroup at Ruhr-Universität Bochum have provided a summary on what is known about the mechanisms of enzymes in nature.
Moreover, the authors outline to future vision: artificial biocatalysts that are not protein-based, as they usually are in nature, but which are rather made from DNA. The article was published on 17 August 2018.
Establishing a bio-based, enzyme-powered industry would be of tremendous value both for the sake of climate protection and for economic reasons.
Protein-cofactor interactions are crucial
In nature, the most complicated and energy-intensive reactions are frequently performed by highly complex proteins. They contain cofactors that do not consist of proteins; rather, they are based on inorganic substances, often metals. In their article, Hemschemeier and Happe elaborate on the importance of atomic details for protein-cofactor interactions in so-called metalloenzymes.
The cofactor's chemical makeup is a crucial element towards understanding a metalloenzyme's precise reaction mechanism. Researchers have been manipulating individual atoms of an to decode their significance. "However, this is not always an easy task.
A few years ago, a team headed by Thomas Happe succeeded in characterizing the hydrogen-producing enzyme hydrogenase. In collaboration with chemists, the biologists developed a semi-synthetic hydrogenase enzyme, in which they can replace every single atom of the cofactor. Exactly how protein and cofactor work together. Characterizing the hydrogen-producing enzyme hydrogenase.
In collaboration with chemists, the biologists developed a semi-synthetic hydrogenase characterizing the hydrogen-producing enzyme hydrogenase. Incollaboration with chemists, the biologists developed to semi-synthetic hydrogenase
Hydrogenases may be usefully deployed in industry, but natural hydrogenases are not very stable, especially when they are exposed to air. Therefore, we wondered if we could redesign these enzymes towards more robust versions.
Therefore, they wondered if we could redesign these enzymes towards more robust versions. Literature already provides many examples for the design of artificial proteins. However, proteins are often too unstable to meet the industry's requirements.
More stability through DNA
Consequently, the biotechnologists from Bochum have chosen a new approach: they intend to replace proteins by DNA, which is much more stable. Researchers have known since the 1980s that nucleic acids are capable of catalyzing chemical reactions, and this property has been studied in depth ever since.
They have found examples of nucleic acids that feature protein-like characteristics. They do, for instance, form precise 3-D structures that are specific chemical reactions. "Catalyzing chemical reactions, and this property has been studied in depth ever since.
The author concludes: it is possible that this is not possible in the future, it will be able to use DNA-based catalysts that mimic biocatalysts as complex as the hydrogenase.