Protecting biocatalysts from oxygen

Protecting biocatalysts from oxygen

Certain enzymes from bacteria and algae can produce molecular hydrogen from protons and electrons – an energy carrier on which many hopes are riding. All they need for this purpose is light energy. The major obstacle to their use is that they are destroyed by contact with oxygen. An interdisciplinary research team from the RESOLV cluster of excellence at Ruhr University Bochum, Germany, has succeeded in genetically modifying a hydrogen-producing enzyme so that it is protected from oxygen. The researchers headed by Professor Thomas Happe, head of the Photobiotechnology group, Professor Lars Schäfer and Professor Ulf-Peter Apfel report in the journal ACS Catalysis of 28 December 2022.

For the energy transition to succeed, we require environmentally friendly energy carriers. Hydrogen could be one such source if it could be produced on a large scale in a carbon-neutral way. Researchers are relying on enzymes that occur naturally in certain algae and bacteria, to name just a few. “Due to their high conversion rates, they serve as a biological blueprint for the design of future hydrogen catalysts,” explains lead author Andreas Rutz. But their unique active site, known as the H-cluster, degrades on contact with oxygen. “This is the greatest hurdle in hydrogen research,” says Rutz.

Oxygen resistance increases considerably

The recently discovered [FeFe] hydrogenase called CbA5H is the only known enzyme of its class that can protect itself from oxygen by a molecular protection mechanism. However, a fraction of the hydrogenase is also destroyed in the process. To remedy this problem, the researchers specifically exchanged a building block of the enzyme. This genetic modification meant they could significantly increase the oxygen resistance of the hydrogenase.

The teams used site-directed mutagenesis in combination with electrochemistry, infrared spectroscopy and molecular dynamics simulations to better understand the kinetics of the transformation at the atomic level. “We intend to use our findings to understand how local modifications of protein structure can significantly influence protein dynamics and how they can effectively control the reactivity of inorganic centres,” explain Lars Schäfer and Ulf-Peter Apfel.


The research was funded by the European Union as part of the Marie Sklodowska-Curie programme (grant no. 801459 - FP-RESOMUS) and the German Research Foundation as part of the Ruhr Explores Solvation RESOLV Cluster of Excellence (EXC 2033 - 390677874).

Andreas Rutz et al.: Increasing the O2 resistance of the [FeFe]-hydrogenase CbA5H through enhanced protein flexibility, in: ACS Catalysis, 2023, DOI: 10.1021/acscatal.2c04031,
Attached files
  • Lars Schäfer, Thomas Happe and Ulf-Peter Apfel (from left) collaborated on the current study.© RUB, MarquardThis image may only be used in the context of the press release "Protecting biocatalysts from oxygen" published by RUB on 11. January 2023.
Regions: Europe, Germany
Keywords: Science, Life Sciences, Energy


For well over a decade, in my capacity as a researcher, broadcaster, and producer, I have relied heavily on Alphagalileo.
All of my work trips have been planned around stories that I've found on this site.
The under embargo section allows us to plan ahead and the news releases enable us to find key experts.
Going through the tailored daily updates is the best way to start the day. It's such a critical service for me and many of my colleagues.
Koula Bouloukos, Senior manager, Editorial & Production Underknown
We have used AlphaGalileo since its foundation but frankly we need it more than ever now to ensure our research news is heard across Europe, Asia and North America. As one of the UK’s leading research universities we want to continue to work with other outstanding researchers in Europe. AlphaGalileo helps us to continue to bring our research story to them and the rest of the world.
Peter Dunn, Director of Press and Media Relations at the University of Warwick
AlphaGalileo has helped us more than double our reach at SciDev.Net. The service has enabled our journalists around the world to reach the mainstream media with articles about the impact of science on people in low- and middle-income countries, leading to big increases in the number of SciDev.Net articles that have been republished.
Ben Deighton, SciDevNet

We Work Closely With...

  • BBC
  • The Times
  • National Geographic
  • The University of Edinburgh
  • University of Cambridge
Copyright 2023 by AlphaGalileo Terms Of Use Privacy Statement