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

Author

Listed:
  • 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)
    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 (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.

Suggested Citation

  • 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, 2024. "Identifying a key spot for electron mediator-interaction to tailor CO dehydrogenase’s affinity," Nature Communications, Nature, vol. 15(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-46909-1
    DOI: 10.1038/s41467-024-46909-1
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    References listed on IDEAS

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    1. Yuri Choi & Rashmi Mehrotra & Sang-Hak Lee & Trang Vu Thien Nguyen & Inhui Lee & Jiyeong Kim & Hwa-Young Yang & Hyeonmyeong Oh & Hyunwoo Kim & Jae-Won Lee & Yong Hwan Kim & Sung-Yeon Jang & Ji-Wook Ja, 2022. "Bias-free solar hydrogen production at 19.8 mA cm−2 using perovskite photocathode and lignocellulosic biomass," Nature Communications, Nature, vol. 13(1), pages 1-9, December.
    2. Christopher C. Page & Christopher C. Moser & Xiaoxi Chen & P. Leslie Dutton, 1999. "Natural engineering principles of electron tunnelling in biological oxidation–reduction," Nature, Nature, vol. 402(6757), pages 47-52, November.
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