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2H-Thiopyran-2-thione sulfine, a compound for converting H2S to HSOH/H2S2 and increasing intracellular sulfane sulfur levels

Author

Listed:
  • Qi Cui

    (Brown University)

  • Meg Shieh

    (Brown University)

  • Tony W. Pan

    (Brown University)

  • Akiyuki Nishimura

    (National Institutes of Natural Sciences)

  • Tetsuro Matsunaga

    (Tohoku University Graduate School of Medicine)

  • Shane S. Kelly

    (Pacific Northwest National Laboratory)

  • Shi Xu

    (Brown University)

  • Minkyung Jung

    (Tohoku University Graduate School of Medicine)

  • Seiryo Ogata

    (Tohoku University Graduate School of Medicine)

  • Masanobu Morita

    (Tohoku University Graduate School of Medicine)

  • Jun Yoshitake

    (Tohoku University Graduate School of Medicine)

  • Xiaoyan Chen

    (Brown University)

  • Jerome R. Robinson

    (Brown University)

  • Wei-Jun Qian

    (Pacific Northwest National Laboratory)

  • Motohiro Nishida

    (National Institutes of Natural Sciences
    Kyushu University)

  • Takaaki Akaike

    (Tohoku University Graduate School of Medicine)

  • Ming Xian

    (Brown University)

Abstract

Reactive sulfane sulfur species such as persulfides (RSSH) and H2S2 are important redox regulators and closely linked to H2S signaling. However, the study of these species is still challenging due to their instability, high reactivity, and the lack of suitable donors to produce them. Herein we report a unique compound, 2H-thiopyran-2-thione sulfine (TTS), which can specifically convert H2S to HSOH, and then to H2S2 in the presence of excess H2S. Meanwhile, the reaction product 2H-thiopyran-2-thione (TT) can be oxidized to reform TTS by biological oxidants. The reaction mechanism of TTS is studied experimentally and computationally. TTS can be conjugated to proteins to achieve specific delivery, and the combination of TTS and H2S leads to highly efficient protein persulfidation. When TTS is applied in conjunction with established H2S donors, the corresponding donors of H2S2 (or its equivalents) are obtained. Cell-based studies reveal that TTS can effectively increase intracellular sulfane sulfur levels and compensate for certain aspects of sulfide:quinone oxidoreductase (SQR) deficiency. These properties make TTS a conceptually new strategy for the design of donors of reactive sulfane sulfur species.

Suggested Citation

  • Qi Cui & Meg Shieh & Tony W. Pan & Akiyuki Nishimura & Tetsuro Matsunaga & Shane S. Kelly & Shi Xu & Minkyung Jung & Seiryo Ogata & Masanobu Morita & Jun Yoshitake & Xiaoyan Chen & Jerome R. Robinson , 2024. "2H-Thiopyran-2-thione sulfine, a compound for converting H2S to HSOH/H2S2 and increasing intracellular sulfane sulfur levels," Nature Communications, Nature, vol. 15(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-46652-7
    DOI: 10.1038/s41467-024-46652-7
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    References listed on IDEAS

    as
    1. Takaaki Akaike & Tomoaki Ida & Fan-Yan Wei & Motohiro Nishida & Yoshito Kumagai & Md. Morshedul Alam & Hideshi Ihara & Tomohiro Sawa & Tetsuro Matsunaga & Shingo Kasamatsu & Akiyuki Nishimura & Masano, 2017. "Cysteinyl-tRNA synthetase governs cysteine polysulfidation and mitochondrial bioenergetics," Nature Communications, Nature, vol. 8(1), pages 1-15, December.
    2. Tetsuro Matsunaga & Hirohito Sano & Katsuya Takita & Masanobu Morita & Shun Yamanaka & Tomohiro Ichikawa & Tadahisa Numakura & Tomoaki Ida & Minkyung Jung & Seiryo Ogata & Sunghyeon Yoon & Naoya Fujin, 2023. "Supersulphides provide airway protection in viral and chronic lung diseases," Nature Communications, Nature, vol. 14(1), pages 1-25, December.
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