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Abstract The green leaf volatiles (GLVs)Z‐3‐hexen‐1‐ol (Z3‐HOL) andZ‐3‐hexenyl acetate (Z3‐HAC) are airborne infochemicals released from damaged plant tissues that induce defenses and developmental responses in receiver plants, but little is known about their mechanism of action. We found that Z3‐HOL and Z3‐HAC induce similar but distinctive physiological and signaling responses in tomato seedlings and cell cultures. In seedlings, Z3‐HAC showed a stronger root growth inhibition effect than Z3‐HOL. In cell cultures, the two GLVs induced distinct changes in MAP kinase (MAPK) activity and proton fluxes as well as rapid and massive changes in the phosphorylation status of proteins within 5 min. Many of these phosphoproteins are involved in reprogramming the proteome from cellular homoeostasis to stress and include pattern recognition receptors, a receptor‐like cytoplasmic kinase, MAPK cascade components, calcium signaling proteins and transcriptional regulators. These are well‐known components of damage‐associated molecular pattern (DAMP) signaling pathways. These rapid changes in the phosphoproteome may underly the activation of defense and developmental responses to GLVs. Our data provide further evidence that GLVs function like DAMPs and indicate that GLVs coopt DAMP signaling pathways. 

Bioorthogonal reactions are powerful tools for studying and manipulating biological systems, yet achieving precise spatial and temporal control remains a major challenge. Here, we introduce cyclopropanol (CPol) as a compact, energy-loaded warhead that remains inert under physiological conditions and is selectively activated by mild electrochemical stimuli. This strategy generates reactive β-haloketone moieties in situ, enabling dual-function bioconjugation for cellular labeling and proteomic analysis. Upon oxidative ring opening, CPol preferentially modifies carboxylic acid-containing residues, such as glutamate and aspartate, rather than the expected tyrosine or tryptophan. The electrochemical activation of CPol is biocompatible in living systems, enabling direct protein labeling, real-time visualization with a fluorogenic CPol probe, and selective targeting of membrane-associated and cytoplasmic proteins with a choline-derived probe through integration into cellular phosphatidylcholine metabolism. Coupling bioorthogonality with electrochemical control, this approach enables precise protein profiling, live-cell imaging, and broader applications in chemical biology.