Current status of carbon monoxide dehydrogenases (CODH) and their potential for electrochemical applications

Bährle, Rebecca; Böhnke, Stefanie; Englhard, Jonas; Bachmann, Julien; Perner, Mirjam

doi:10.1186/s40643-023-00705-9

Cited by 6 publications

(1 citation statement)

References 187 publications

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“…This is expected since Mo-CODH are limited to CO oxidation. 56,57 The redox potential of the enzyme is much more positive than that of CO 2 /CO, making the CO 2 reduction reaction thermodynamically unfavorable.…”

Section: Supplemental Notesmentioning

confidence: 99%

Quinone extraction drives atmospheric carbon monoxide oxidation in bacteria

Kropp,

Gillett,

Venugopal

et al. 2024

Preprint

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Diverse bacteria and archaea use atmospheric carbon monoxide (CO) as an energy source during long-term survival. This process enhances the biodiversity of soil and marine ecosystems globally and removes 250 million tonnes of a toxic, climate-relevant pollutant from the atmosphere each year. Bacteria use [MoCu]-carbon monoxide dehydrogenases (Mo-CODH) to convert CO to carbon dioxide, then transfer the liberated high-energy electrons to the aerobic respiratory chain. However, given no high-affinity Mo-CODH has been purified, it is unknown how these enzymes oxidise CO at low concentrations and interact with the respiratory chain. Here we resolve these knowledge gaps by analysing Mo-CODH (CoxSML) and its hypothetical partner CoxG fromMycobacterium smegmatis. Kinetic and electrochemical analyses show purified Mo-CODH is a highly active high-affinity enzyme (Km= 139 nM,kcat= 54.2 s-1). Based on its 1.85 Å resolution cryoEM structure, Mo-CODH forms a CoxSML homodimer similar to characterised low-affinity homologs, but has distinct active site coordination and narrower gas channels that may modulate affinity. We provide structural, biochemical, and genetic evidence that Mo-CODH transfers CO-derived electrons to the aerobic respiratory chainviathe membrane-bound menaquinone-binding protein CoxG. Consistently, CoxG is required for CO-driven respiration, extracts menaquinone from mycobacterial membranes, and binds quinones in a hydrophobic pocket. Finally, we show that Mo-CODH and CoxG genetically and structurally associate in diverse bacteria and archaea. These findings reveal the basis of a biogeochemically and ecologically important process, while demonstrating that the newly discovered process of long-range quinone transport is a general mechanism of energy conservation, which convergently evolved on multiple occasions.

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Section: Supplemental Notesmentioning

confidence: 99%

Quinone extraction drives atmospheric carbon monoxide oxidation in bacteria

Kropp,

Gillett,

Venugopal

et al. 2024

Preprint

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Rational Design of Earth‐Abundant Catalysts toward Sustainability

Guo,

Haghshenas,

Jiao

et al. 2024

Advanced Materials

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Catalysis is crucial for clean energy, green chemistry, and environmental remediation, but traditional methods rely on expensive and scarce precious metals. This review addresses this challenge by highlighting the promise of earth‐abundant catalysts and the recent advancements in their rational design. Innovative strategies such as physics‐inspired descriptors, high‐throughput computational techniques, and artificial intelligence (AI)‐assisted design with machine learning (ML) are explored, moving beyond time‐consuming trial‐and‐error approaches. Additionally, biomimicry, inspired by efficient enzymes in nature, offers valuable insights. This review systematically analyses these design strategies, providing a roadmap for developing high‐performance catalysts from abundant elements. Clean energy applications (water splitting, fuel cells, batteries) and green chemistry (ammonia synthesis, CO2 reduction) are targeted while delving into the fundamental principles, biomimetic approaches, and current challenges in this field. The way to a more sustainable future is paved by overcoming catalyst scarcity through rational design.

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