Tungsten-dependent formate dehydrogenase of Cupriavidus necator as an O2-tolerant biocatalyst for cofactor regeneration and CO2 fixation
Cupriavidus necator’s tungsten-dependent NAD + -reducing formate dehydrogenase ( Cn FDW) has strong potential as a cofactor-recycling biocatalyst, as it remains active under ambient air (∼21% O 2 ) and elevated O 2 levels (up to 50%). Using formate as a clean reductant, Cn FDW enables efficient NADH regeneration for diverse oxidoreductases and oxygenases under aerobic conditions, achieving complete conversion of representative substrates within 8 h and retaining high product yields (92–87%) upon a 10-fold increase in reaction volume and higher substrate concentrations. In reverse reaction, coupling of Cn FDW to the O 2 -tolerant NAD + -reducing hydrogenase of C. necator ( Cn SH) enables H 2 -driven CO 2 reduction to formate. In anaerobic conditions, concentrations of up to 64 mM formate were achieved, when using methyl viologen instead of NAD + /H as electron mediator. Overall, these results establish Cn FDW as an O 2 tolerant biocatalyst for both, aerobic cofactor recycling and sustainable H 2 -driven CO 2 valorisation to formate.
Authors
- Lars Lauterbach (ORCID: https://orcid.org/0000-0002-6601-6473)
- Elisabeth Lettau
- Guiyeoul Lim (ORCID: https://orcid.org/0000-0001-5946-2240)
- Donato Calabrese
- Janet Geiermann
Institutions
- University of British Columbia (CA)
- Fraunhofer Institute for Molecular Biology and Applied Ecology (DE)
- RWTH Aachen University (DE)
- The University of Osaka (JP)
Publication Details
- Journal
- Journal of CO2 Utilization
- Published
- 2026-09-11
- DOI
- https://doi.org/10.1016/j.jcou.2026.103562
- Primary Topic
- Metalloenzymes and iron-sulfur proteins
- Type
- article
- Field-Weighted Citation Impact
- 0.00