Bacteria Use Hydrogen to Make Clean Fuel and Fight Climate Change
- Authors
- Sabrina Dezzani, Abdulrahman Alogaidi, Anca Pordea, Simone Morra
- Journal
- Biochemical Journal
- Year
- 2026
- DOI
- 10.1042/BCJ20253323
- Study Type
- Cell Culture
- Outcome
- Neutral
- Peer Reviewed
- Yes
- Country
- United Kingdom
- Health Condition
- Whole Body
TL;DR
Researchers identified a bacterial enzyme complex that both produces and consumes hydrogen, playing a key role in biofuel production and microbial energy metabolism.
Key Finding
Clostridium beijerinckii contains a novel enzyme complex that reversibly links hydrogen and CO2 metabolism through multiple catalytic activities, including hydrogen evolution, formate breakdown, and hydrogen-driven CO2 reduction.
Summary
Researchers studied a bacterial enzyme complex in Clostridium beijerinckii that works with hydrogen and carbon dioxide. The enzyme can perform multiple reactions: it can produce hydrogen gas, break down formate (a chemical compound) into hydrogen and CO2, and use hydrogen to reduce CO2. Understanding this enzyme may help scientists develop better ways to produce biofuels (sustainable fuels made from bacteria) and capture carbon dioxide.
Practical Takeaway
This is basic microbiology research focused on bacterial enzyme function and biofuel production—not a study on hydrogen water for human consumption. While it demonstrates that bacteria can metabolize hydrogen gas in complex ways, it provides no direct evidence about health effects of drinking hydrogen-enriched water in humans.
Abstract
The production of biofuels by bacterial fermentation receives sustained attention due to the need to develop novel circular and sustainable technologies. Clostridium beijerinckii produces both hydrogen (H2) and carbon-based biofuels acetone, butanol, and ethanol (ABE solvents). H2 metabolism in C. beijerinckii is complex and mostly unexplored. Seven hydrogenase genes are contained in the genome, but their exact physiological role is unknown. Here, we report on the characterisation of a novel heterotetrameric soluble enzyme complex composed of an [FeFe]-hydrogenase component stably bound to a formate dehydrogenase subunit, which we name CbFdh/Hyd. We show that the four subunits form a stable complex that can be conveniently overexpressed and purified recombinantly. CbFdh/Hyd is highly sensitive to atmospheric oxygen and displays reversible catalytic features, including H2 evolution, H2 uptake, formate oxidation, and the ability to split formate into H2 and CO2 (formate hydrogen lyase activity, FHL) as well as the opposite reaction, H2-driven CO2 reduction (HDCR). CbFdh/Hyd displays functional and spectroscopic features very similar to Fdh/Hyd complexes previously described in acetogens, suggesting that this enzyme is at the basis of the previously reported unconventional ability of C. beijerinckii to fix CO2 into acetate and butyrate. CbFdh/Hyd could also represent a key player in H2 production metabolism by degrading formate produced from the decarboxylation of pyruvate.