Identifying a key spot for electron mediator-interaction to tailor CO dehydrogenase’s affinity

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 () and Yong Hwan Kim ()
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Suk Min Kim: Ulsan National Institute of Science and Technology (UNIST)
Sung Heuck Kang: Ulsan National Institute of Science and Technology (UNIST)
Jinhee Lee: Ulsan National Institute of Science and Technology (UNIST)
Yoonyoung Heo: Gwanak-gu
Eleni G. Poloniataki: Ulsan National Institute of Science and Technology (UNIST)
Jingu Kang: Ulsan National Institute of Science and Technology (UNIST)
Hye-Jin Yoon: Gwanak-gu
So Yeon Kong: Gwanak-gu
Yaejin Yun: Gwanak-gu
Hyunwoo Kim: Ulsan National Institute of Science and Technology (UNIST)
Jungki Ryu: Ulsan National Institute of Science and Technology (UNIST)
Hyung Ho Lee: Gwanak-gu
Yong Hwan Kim: Ulsan National Institute of Science and Technology (UNIST)

Nature Communications, 2024, vol. 15, issue 1, 1-12

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 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 (kcat). 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.

Date: 2024
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DOI: 10.1038/s41467-024-46909-1

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