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Bochum team engineers artificial hydrogenase for hydrogen production; targeting foundation for industrial manufacturing

Researchers at Ruhr-Universität Bochum (RUB) have engineered a hydrogen-producing enzyme in the test tube that works as efficiently as the original. The protein—a hydrogenase from green algae ( [FeFe]-hydrogenase HYDA1 from Chlamydomonas reinhardtii)—is made up of a protein scaffold and a cofactor.

The researchers have been investigating mechanisms of hydrogen biocatalysis for a number of years. In 2013, the team reported developing semi-synthetic hydrogenases by adding the protein’s biological precursor to a chemically synthesized inactive iron complex.

The cofactor is the reaction center where the substances that react with each other dock. When the researchers added various chemically synthesized substances to the protein scaffold, the cofactor spontaneously assembled.

The team, headed by Dr. Jens Noth and Prof. Dr. Thomas Happe, intends to lay the foundation for artificial, hydrogen-producing enzymes that will one day be manufactured on an industrial level. Hydrogenases are very efficient producers of the potential energy carrier and can do without the expensive precious metal platinum which is currently required for hydrogen synthesis. A paper on the work is published in the journal at the Ruhr-Universität Bochum report the results in the journal Angewandte Chemie.

In nature, the hydrogenase cofactor is made up of iron and sulfur atoms which are bonded in the protein in a unique manner. In the artificial variant, the researchers replaced the native [4FeH] cluster with selenium atoms, which have more than twice as much mass. Using this method, they marked the enzyme’s cofactor and were able to analyze it in more detail.

The tests revealed that the artificial enzyme variant has the same biochemical properties as the original that occurs in nature. With the aid of other biophysical methods, the group intends to figure out the reaction mechanism in more detail that is used by the hydrogenase for the production of hydrogen.

For the purpose of the study, the research group Photobiotechnology headed by Thomas Happe cooperated with the team of Dr. Ulf-Peter Apfel at the Chair of Inorganic Chemistry and the biophysical groups of Prof. Dr. Klaus Gerwert and Prof. Dr. Eckhard Hofmann.

The German Research Foundation financed the project as part of the German-Israeli project cooperation “Nanoengineered optoelectronics with biomaterials and bioinspired assemblies” as well as under the umbrella of the Cluster of Excellence Resolv (EXC1069) and an Emmy Noether Grant (AP242/2-1). Additional funding was supplied by the Volkswagen Foundation (Volkswagen Stiftung) (LigH2t) and “Verband der Chemischen Industrie” (Liebig Grant).


  • Noth, J., Esselborn, J., Güldenhaupt, J., Brünje, A., Sawyer, A., Apfel, U.-P., Gerwert, K., Hofmann, E., Winkler, M. and Happe, T. (2016), “[FeFe]-Hydrogenase with Chalcogenide Substitutions at the H-Cluster Maintains Full H2 Evolution Activity.” Angew. Chem. doi: 10.1002/ange.201511896

  • J. Esselborn, C. Lambertz, A. Adamska-Venkatesh, T. Simmons, G. Berggren, J. Noth, J. Siebel, A. Hemschemeier, V. Artero, E. Reijerse, M. Fontecave, W. Lubitz, T. Happe, (2013) “Spontaneous activation of [FeFe]-hydrogenases by an inorganic [2Fe] active site mimic,” Nature Chemical Biology doi: 10.1038/nchembio.1311


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