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Hydrogen sulfide (H2S) is now recognized as an important biological regulator and signaling agent that is active in many physiological processes and diseases. Understanding the important roles of this emerging signaling molecule has remained challenging, in part due to the limited methods available for detecting endogenous H2S. Here we report two reaction-based ChemiLuminescent Sulfide Sensors, CLSS-1 and CLSS-2, with strong luminescence responses toward H2S (128- and 48-fold, respectively) and H2S detection limits (0.7 ± 0.3, 4.6 ± 2.0 μM, respectively) compatible with biological H2S levels. CLSS-2 is highly selective for H2S over other reactive sulfur, nitrogen, and oxygen species (RSONS) including GSH, Cys, Hcy, S2O3(2–), NO2(–), HNO, ONOO(–), and NO. Despite its similar chemical structure, CLSS-1 displays lower selectivity toward amino acid-derived thiols than CLSS-2. The origin of this differential selectivity was investigated using both computational DFT studies and NMR experiments. Our results suggest a model in which amino acid binding to the hydrazide moiety of the luminol-derived probes provides differential access to the reactive azide in CLSS-1 and CLSS-2, thus eroding the selectivity of CLSS-1 for H2S over Cys and GSH. On the basis of its high selectivity for H2S, we used CLSS-2 to detect enzymatically produced H2S from isolated cystathionine γ-lyase (CSE) enzymes (p &lt; 0.001) and also from C6 cells expressing CSE (p &lt; 0.001). CLSS-2 can readily differentiate between H2S production in active CSE and CSE inhibited with β-cyanoalanine (BCA) in both isolated CSE enzymes (p &lt; 0.005) and in C6 cells (p &lt; 0.005). In addition to providing a highly sensitive and selective reaction-based tool for chemiluminescent H2S detection and quantification, the insights into substrate–probe interactions controlling the selectivity for H2S over biologically relevant thiols may guide the design of other selective H2S detection scaffolds.

journal of the american chemical society

Chemiluminescent Detection of Enzymatically Produced Hydrogen Sulfide: Substrate Hydrogen Bonding Influences Selectivity for H<sub>2</sub>S over Biological Thiols

Chemiluminescent Detection of Enzymatically Produced Hydrogen Sulfide: Substrate Hydrogen Bonding Influences Selectivity for H2S over Biological Thiols

Chemiluminescent Detection of Enzymatically Produced Hydrogen Sulfide: Substrate Hydrogen Bonding Influences Selectivity for H₂S over Biological Thiols