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.

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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
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article
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article

Tungsten-dependent formate dehydrogenase of Cupriavidus necator as an O2-tolerant biocatalyst for cofactor regeneration and CO2 fixation

Lars Lauterbach, Elisabeth Lettau, Guiyeoul Lim, Donato Calabrese et al.
Journal of CO2 Utilization
Metalloenzymes and iron-sulfur proteins
article

Tungsten-dependent formate dehydrogenase of Cupriavidus necator as an O2-tolerant biocatalyst for cofactor regeneration and CO2 fixation

Lars Lauterbach, Elisabeth Lettau, Guiyeoul Lim, Donato Calabrese, Janet Geiermann
article en

Abstract

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.

Journal of CO2 UtilizationVol. 112
University of British Columbia (CA), Fraunhofer Institute for Molecular Biology and Applied Ecology (DE), RWTH Aachen University (DE), The University of Osaka (JP)
Responsible consumption and production
Openalex Percentile: Top 29%
Metalloenzymes and iron-sulfur proteins
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Tungsten-dependent formate dehydrogenase of Cupriavidus necator as an O2-tolerant biocatalyst for cofactor regeneration and CO2 fixation — Lars Lauterbach, Elisabeth Lettau, et al. · Journal of CO2 Utilization (2026) | TGRS Research Map | TGRS