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Trapping of a Mononitrosyl Nonheme Intermediate of Nitric Oxide Reductase by Cryo-Photolysis of Caged Nitric Oxide

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Download Hi-Res ImageDownload to MS-PowerPointCite This:J. Phys. Chem. B 2023, 127, 4, 846-854
    B: Biophysical and Biochemical Systems and Processes

    Trapping of a Mononitrosyl Nonheme Intermediate of Nitric Oxide Reductase by Cryo-Photolysis of Caged Nitric Oxide
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    • Hanae Takeda
      Hanae Takeda
      Graduate School of Life Science, University of Hyogo, Ako, Hyogo 678-1297, Japan
      RIKEN SPring-8 center, Sayo, Hyogo 679-5148, Japan
      More by Hanae Takeda
    • Kanji Shimba
      Kanji Shimba
      Graduate School of Life Science, University of Hyogo, Ako, Hyogo 678-1297, Japan
      RIKEN SPring-8 center, Sayo, Hyogo 679-5148, Japan
      More by Kanji Shimba
    • Masaki Horitani
      Masaki Horitani
      Department of Applied Biochemistry & Food Science, Saga University, Saga 840-8502, Japan
      The United Graduate School of Agricultural Science, Kagoshima University, 1-21-24 Korimoto, Kagoshima 890-0065, Japan
      More by Masaki Horitani
      Orcidhttps://orcid.org/0000-0002-8881-0600
    • Tetsunari Kimura
      Tetsunari Kimura
      Department of Chemistry, Graduate School of Science, Kobe University, Kobe 657-8501, Japan
      More by Tetsunari Kimura
    • Takashi Nomura
      Takashi Nomura
      Graduate School of Life Science, University of Hyogo, Ako, Hyogo 678-1297, Japan
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    • Minoru Kubo
      Minoru Kubo
      Graduate School of Life Science, University of Hyogo, Ako, Hyogo 678-1297, Japan
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    • Yoshitsugu Shiro*
      Yoshitsugu Shiro
      Graduate School of Life Science, University of Hyogo, Ako, Hyogo 678-1297, Japan
      *Yoshitsugu Shiro. E-mail: [email protected]
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      Orcidhttps://orcid.org/0000-0003-0695-8327
    • Takehiko Tosha*
      Takehiko Tosha
      Graduate School of Life Science, University of Hyogo, Ako, Hyogo 678-1297, Japan
      RIKEN SPring-8 center, Sayo, Hyogo 679-5148, Japan
      *Takehiko Tosha. E-mail: [email protected]
      More by Takehiko Tosha
      Orcidhttps://orcid.org/0000-0002-8971-0759
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    The Journal of Physical Chemistry B

    Cite this: J. Phys. Chem. B 2023, 127, 4, 846–854
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    https://doi.org/10.1021/acs.jpcb.2c05852
    Published January 5, 2023
    Copyright © 2023 American Chemical Society
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    Abstract

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    Characterization of short-lived reaction intermediates is essential for elucidating the mechanism of the reaction catalyzed by metalloenzymes. Here, we demonstrated that the photolysis of a caged compound under cryogenic temperature followed by thermal annealing is an invaluable technique for trapping of short-lived reaction intermediates of metalloenzymes through the study of membrane-integrated nitric oxide reductase (NOR) that catalyzes reductive coupling of two NO molecules to N2O at its heme/nonheme FeB binuclear center. Although NO produced by the photolysis of caged NO did not react with NOR under cryogenic temperature, annealing to ∼160 K allowed NO to diffuse and react with NOR, which was evident from the appearance of EPR signals assignable to the S = 3/2 state. This indicates that the nonheme FeB-NO species can be trapped as the intermediate. Time-resolved IR spectroscopy with the use of the photolysis of caged NO as a reaction trigger showed that the intermediate formed at 10 μs gave the NO stretching frequency at 1683 cm–1 typical of nonheme Fe-NO, confirming that the combination of the cryo-photolysis of caged NO and annealing enabled us to trap the reaction intermediate. Thus, the cryo-photolysis of the caged compound has great potential for the characterization of short-lived reaction intermediates.

    Copyright © 2023 American Chemical Society

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    Supporting Information

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    • EPR spectra of photolyzed caged NO (PDF)

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    This article is cited by 4 publications.

    1. Masaru KATO, Ichizo YAGI. Protein Film Electrochemistry and Spectroscopic Measurements of Transmembrane Metalloenzymes. Vacuum and Surface Science 2024, 67 (10) , 483-488. https://doi.org/10.1380/vss.67.483
    2. Therese Albert, Arun Kumar, Jonathan Caranto, Pierre Moënne-Loccoz. Vibrational analyses of the reaction of oxymyoglobin with NO using a photolabile caged NO donor at cryogenic temperatures. Journal of Inorganic Biochemistry 2024, 258 , 112633. https://doi.org/10.1016/j.jinorgbio.2024.112633
    3. Alberto Mezzetti. Photobiological systems studied by time-resolved infrared spectroscopy (2021–2022). 2023, 126-158. https://doi.org/10.1039/BK9781837672301-00126
    4. Jill B. Harland, Subhra Samanta, Nicolai Lehnert. Bacterial nitric oxide reductase (NorBC) models employing click chemistry. Journal of Inorganic Biochemistry 2023, 246 , 112280. https://doi.org/10.1016/j.jinorgbio.2023.112280
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    The Journal of Physical Chemistry B

    Cite this: J. Phys. Chem. B 2023, 127, 4, 846–854
    Click to copy citationCitation copied!
    https://doi.org/10.1021/acs.jpcb.2c05852
    Published January 5, 2023
    Copyright © 2023 American Chemical Society
    Request reuse permissions

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