Identifying a key spot for electron mediator-interaction to tailor CO dehydrogenase’s affinity
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 enz...
| Main Authors: | , , , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
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Nature Portfolio
2024-03-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-024-46909-1 |
| _version_ | 1797233459793494016 |
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| author | Suk Min Kim Sung Heuck Kang Jinhee Lee Yoonyoung Heo Eleni G. Poloniataki Jingu Kang Hye-Jin Yoon So Yeon Kong Yaejin Yun Hyunwoo Kim Jungki Ryu Hyung Ho Lee Yong Hwan Kim |
| author_facet | Suk Min Kim Sung Heuck Kang Jinhee Lee Yoonyoung Heo Eleni G. Poloniataki Jingu Kang Hye-Jin Yoon So Yeon Kong Yaejin Yun Hyunwoo Kim Jungki Ryu Hyung Ho Lee Yong Hwan Kim |
| author_sort | Suk Min Kim |
| collection | DOAJ |
| description | 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 cat). Viologen-complexed structures reveal the pivotal positions of surface phenylalanine residues, serving as external conduits for the D-cluster to/from viologen. One variant (R57G/N59L/A559W) can 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. |
| first_indexed | 2024-04-24T16:16:31Z |
| format | Article |
| id | doaj.art-64c19e8a4f2a4362a0d29cf896a48375 |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-04-24T16:16:31Z |
| publishDate | 2024-03-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-64c19e8a4f2a4362a0d29cf896a483752024-03-31T11:25:07ZengNature PortfolioNature Communications2041-17232024-03-0115111210.1038/s41467-024-46909-1Identifying a key spot for electron mediator-interaction to tailor CO dehydrogenase’s affinitySuk Min Kim0Sung Heuck Kang1Jinhee Lee2Yoonyoung Heo3Eleni G. Poloniataki4Jingu Kang5Hye-Jin Yoon6So Yeon Kong7Yaejin Yun8Hyunwoo Kim9Jungki Ryu10Hyung Ho Lee11Yong Hwan Kim12School of Energy and Chemical Engineering, Ulsan National Institute of Science and Technology (UNIST)School of Energy and Chemical Engineering, Ulsan National Institute of Science and Technology (UNIST)School of Energy and Chemical Engineering, Ulsan National Institute of Science and Technology (UNIST)Department of Chemistry, College of Natural Sciences, Seoul National University, 1 Gwanak-ro, Gwanak-guSchool of Energy and Chemical Engineering, Ulsan National Institute of Science and Technology (UNIST)School of Energy and Chemical Engineering, Ulsan National Institute of Science and Technology (UNIST)Department of Chemistry, College of Natural Sciences, Seoul National University, 1 Gwanak-ro, Gwanak-guDepartment of Chemistry, College of Natural Sciences, Seoul National University, 1 Gwanak-ro, Gwanak-guDepartment of Chemistry, College of Natural Sciences, Seoul National University, 1 Gwanak-ro, Gwanak-guSchool of Energy and Chemical Engineering, Ulsan National Institute of Science and Technology (UNIST)School of Energy and Chemical Engineering, Ulsan National Institute of Science and Technology (UNIST)Department of Chemistry, College of Natural Sciences, Seoul National University, 1 Gwanak-ro, Gwanak-guSchool of Energy and Chemical Engineering, Ulsan National Institute of Science and Technology (UNIST)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 cat). Viologen-complexed structures reveal the pivotal positions of surface phenylalanine residues, serving as external conduits for the D-cluster to/from viologen. One variant (R57G/N59L/A559W) can 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.https://doi.org/10.1038/s41467-024-46909-1 |
| spellingShingle | Suk Min Kim Sung Heuck Kang Jinhee Lee Yoonyoung Heo Eleni G. Poloniataki Jingu Kang Hye-Jin Yoon So Yeon Kong Yaejin Yun Hyunwoo Kim Jungki Ryu Hyung Ho Lee Yong Hwan Kim Identifying a key spot for electron mediator-interaction to tailor CO dehydrogenase’s affinity Nature Communications |
| title | Identifying a key spot for electron mediator-interaction to tailor CO dehydrogenase’s affinity |
| title_full | Identifying a key spot for electron mediator-interaction to tailor CO dehydrogenase’s affinity |
| title_fullStr | Identifying a key spot for electron mediator-interaction to tailor CO dehydrogenase’s affinity |
| title_full_unstemmed | Identifying a key spot for electron mediator-interaction to tailor CO dehydrogenase’s affinity |
| title_short | Identifying a key spot for electron mediator-interaction to tailor CO dehydrogenase’s affinity |
| title_sort | identifying a key spot for electron mediator interaction to tailor co dehydrogenase s affinity |
| url | https://doi.org/10.1038/s41467-024-46909-1 |
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