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- W4377013655 abstract "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 Ch CODHs ( 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 exhibited a ten-fold increase in ethyl viologen affinity relative to the wild-type without sacrificing the turn-over rate ( k cat ). Viologen-complexed structures revealed the pivotal positions of surface phenylalanine residues, serving as external conduits for the D-cluster. One variant (G57/L59/W559) could treat a broad spectrum of waste gases (from steel-process and plastic-gasification) containing O 2 . Decoding mediator interactions will facilitate the development of industrially high-efficient biocatalysts encompassing gas-utilizing enzymes." @default.
- W4377013655 created "2023-05-19" @default.
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- W4377013655 date "2023-05-18" @default.
- W4377013655 modified "2023-09-30" @default.
- W4377013655 title "Identifying a key spot for mediator-interaction to tailor CO dehydrogenase’s affinity" @default.
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- W4377013655 doi "https://doi.org/10.21203/rs.3.rs-2847324/v1" @default.
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