| Autor: |
Suk Min Kim, Sung Heuck Kang, Jinhee Lee, Yoonyoung Heo, Ho Won Hwang, Eleni G. Poloniataki, Hye-Jin Yoon, Hyung Ho Lee, Yong Hwan Kim |
| Rok vydání: |
2023 |
| DOI: |
10.21203/rs.3.rs-2847324/v1 |
| Popis: |
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 exhibited a ten-fold increase in ethyl viologen affinity relative to the wild-type without sacrificing the turn-over rate (kcat). 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 O2. Decoding mediator interactions will facilitate the development of industrially high-efficient biocatalysts encompassing gas-utilizing enzymes. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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