ArticleNature communications2024
Identifying a key spot for electron mediator-interaction to tailor CO dehydrogenase's affinity.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
7 citing papers in PubMed.
- An unexpected alternative viologen electron mediator site in tungsten-containing formate dehydrogenase.FEBS letters · 2026Article
- Understanding the Catalytic Determinant role of Diaphorase-Like Subunit in Formate Dehydrogenases via Redox Couples.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Molecular Access Engineering for Microbial Biocatalysis: from Enzyme Tunnels to Microbial Cell Factories.Journal of microbiology and biotechnology · 2026Review
- Integrated chaperone engineering and process optimization enable enhanced production of ChCODH-II A559W in Escherichia coli.World journal of microbiology & biotechnology · 2026Article
- Use of Substrate Analogues and X-ray spectroscopy Reveals an all Ferrous C-Cluster in CO Dehydrogenase.bioRxiv : the preprint server for biology · 2026Article
- Fortification of FeS Clusters Reshapes Anaerobic CO Dehydrogenase into an Air-Viable Enzyme Through Multilayered Sealing of OAngewandte Chemie (International ed. in English) · 2025Article
- Insights into the Role of the D-Cluster in [NiFe]-CODH from Rhodospirillum Rubrum.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
Corrections and comments
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Authors and funding
13 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Fe‒S cluster-harboring enzymes, such as carbon monoxide dehydrogenases (CODH), employ sophisticated artificial electron mediators like viologens to serve as potent biocatalysts capable of cleaning-up industrial off-gases at stunning reaction rates. Unraveling the interplay between these enzymes and their associated mediators is essential for improving the efficiency of CODHs. Here we show the electron mediator-interaction site on ChCODHs (Ch, Carboxydothermus hydrogenoformans) using a systematic approach that leverages the viologen-reactive characteristics of superficial aromatic residues. By enhancing mediator-interaction (R57G/N59L) near the D-cluster, the strategically tailored variants exhibit a ten-fold increase in ethyl viologen affinity relative to the wild-type without sacrificing the turn-over rate (k
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.