Switching ON Hydrogen Sulfide: A Chemogenetic Toolkit for Spatially Resolved H 2 S Manipulation
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Hydrogen sulfide (H 2 S) is emerging as a multifaceted signalling molecule that shapes energy metabolism, vascular tone, cancer biology and neurodegeneration. Although fluorescent and genetically encoded sensors now allow real-time H 2 S imaging, tools for selective control of intracellular H 2 S remain scarce. Here we benchmark two substrate-based chemogenetic enzymes—the yeast D-amino-acid oxidase (mDAAO) and the Salmonella typhimurium D-cysteine desulfhydrase (stDCyD)—for controlled H 2 S production. Both enzymes catalyse the conversion of D-cysteine to H 2 S, yet only mDAAO concomitantly generates hydrogen peroxide, introducing an unwanted oxidative signal. In contrast, stDCyD produces exclusively H 2 S, thereby offering a clean and efficient means to elevate intracellular H 2 S in vitro . Our data position stDCyD as the superior chemogenetic actuator for dissecting H 2 S biology without confounding redox artefacts.
