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A 2.2 Å cryoEM structure of a quinol-dependent NO Reductase shows close similarity to respiratory oxidases

Author

Listed:
  • Alex J. Flynn

    (University of Leeds
    University of Leeds)

  • Svetlana V. Antonyuk

    (University of Liverpool)

  • Robert R. Eady

    (University of Liverpool)

  • Stephen P. Muench

    (University of Leeds
    University of Leeds)

  • S. Samar Hasnain

    (University of Liverpool)

Abstract

Quinol-dependent nitric oxide reductases (qNORs) are considered members of the respiratory heme-copper oxidase superfamily, are unique to bacteria, and are commonly found in pathogenic bacteria where they play a role in combating the host immune response. qNORs are also essential enzymes in the denitrification pathway, catalysing the reduction of nitric oxide to nitrous oxide. Here, we determine a 2.2 Å cryoEM structure of qNOR from Alcaligenes xylosoxidans, an opportunistic pathogen and a denitrifying bacterium of importance in the nitrogen cycle. This high-resolution structure provides insight into electron, substrate, and proton pathways, and provides evidence that the quinol binding site not only contains the conserved His and Asp residues but also possesses a critical Arg (Arg720) observed in cytochrome bo3, a respiratory quinol oxidase.

Suggested Citation

  • Alex J. Flynn & Svetlana V. Antonyuk & Robert R. Eady & Stephen P. Muench & S. Samar Hasnain, 2023. "A 2.2 Å cryoEM structure of a quinol-dependent NO Reductase shows close similarity to respiratory oxidases," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-39140-x
    DOI: 10.1038/s41467-023-39140-x
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    References listed on IDEAS

    as
    1. F. Kolbe & S. Safarian & Ż. Piórek & S. Welsch & H. Müller & H. Michel, 2021. "Cryo-EM structures of intermediates suggest an alternative catalytic reaction cycle for cytochrome c oxidase," Nature Communications, Nature, vol. 12(1), pages 1-11, December.
    2. Svetlana V. Antonyuk & Cong Han & Robert R. Eady & S. Samar Hasnain, 2013. "Structures of protein–protein complexes involved in electron transfer," Nature, Nature, vol. 496(7443), pages 123-126, April.
    3. Takanori Nakane & Abhay Kotecha & Andrija Sente & Greg McMullan & Simonas Masiulis & Patricia M. G. E. Brown & Ioana T. Grigoras & Lina Malinauskaite & Tomas Malinauskas & Jonas Miehling & Tomasz Ucha, 2020. "Single-particle cryo-EM at atomic resolution," Nature, Nature, vol. 587(7832), pages 152-156, November.
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