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

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, Wei-Jun Qian, Motohiro Nishida, Takaaki Akaike () and Ming Xian ()
Additional contact information
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
Takaaki Akaike: Tohoku University Graduate School of Medicine
Ming Xian: Brown University

Nature Communications, 2024, vol. 15, issue 1, 1-13

Abstract: 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.

Date: 2024
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DOI: 10.1038/s41467-024-46652-7

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