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Reactive sulfane sulfur species such as persulfides (RSSH) and H₂S₂are 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 H₂S₂in the presence of excess H₂S. Meanwhile, the reaction product2H-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.