There are high hopes for hydrogen as the key to the energy transition. A specific enzyme group found in algae and in bacteria can produce molecular hydrogen simply by catalyzing protons and electrons. However, the enzyme group is so sensitive to oxygen that commercial use of the hydrogen produced by this process as a green energy source is not yet possible.
Researchers at the Cluster of Excellence RESOLV and the Research Training Group Microbial Substrate Conversion at Ruhr University Bochum increased the oxygen stability of a hydrogen-producing enzyme by genetically generated channel blockages.
The researchers working with Professor Thomas Happe, head of the Photobiotechnology group, Professor Lars Schäfer, Professor Eckhard Hofmann and Professor Ulf-Peter Apfel published their findings in the journal ChemSusChem on 13 October 2023.
Blocked channels improve oxygen stability
A metalloenzyme with particularly high catalytic turnover rates of molecular hydrogen is called [FeFe] hydrogenase. “The turnover of hydrogen takes place at the active site, the H-cluster, inside the enzyme,” explains Happe. “The hydrogen produced inside then travels through channels to exit the enzyme.”
“Conversely, if the enzyme is exposed to molecular oxygen, the oxygen also uses specific channels to travel from the enzyme surface up to the H-cluster,” adds first author Claudia