Correspondence on “Fortification of FeS Clusters Reshapes Anaerobic CO Dehydrogenase Into an Air‐Viable Enzyme Through Multilayered Sealing of O 2 Tunnels”
Year: 2026
Type: letter
Abstract: ABSTRACT In their recent communication in Angewandte Chemie ( 10.1002/anie.202508565 ), Suk Min Kim and coworkers have described the effect of modifying the gas channels of the CO dehydrogenase II from Carboxydothermus hydrogenoformans , an enzyme that oxidizes reversibly CO into CO 2 . Their goal was to use mutagenesis to slow down the arrival of O 2 at the active site. They reported a large increase in the resistance against oxygen, one of the major barriers to the application of this extremely fast and efficient enzyme in biotechnological devices, with an increase in the IC 50 of more than two orders of magnitudes for some variants, with only a minor impact on the affinity of the enzyme for CO. We have produced the same variants, and characterized them in depth using Protein Film Electrochemistry. We used an approach that has proven very useful to learn and understand about the reactivity of CO dehydrogenases (and other redox enzymes like hydrogenases) with O 2 . We found that, contrary to the claims by Kim and coworkers, the A559W and the A559W/V610H mutants are not more resistant than the wild type against oxygen.
DOI: 10.1002/anie.1942100
Language: English
Field: Energy
Domain: Physical Sciences
Open Access status: green
Awards: Rational design of efficient energy and charge transfer in biophotoelectrodes for direct conversion of CO2 into fuel, Propelling CO2 conversion to e-fuels, solar-fuels and e-chemicals beyond the state-of-the-art, Long Range Control of Reactivity in CO Dehydrogenases, G4888527211, Protection of O2 Sensitive Catalysts Under Reductive Conditions, Mechanistic studies of CO 2 reduction: exploration of the biodiversity of CO dehydrogenases, Electrobiocatalytic cascade for bulk reduction of CO2 to CO coupled to fermentative production of high value diamine monomers
OpenAlex ID: W7162187653