Valdiazen Derivatives for Chemoproteomic Studies in Burkholderia cenocepacia H111

Quorum sensing (QS) allows bacteria to coordinate community‐wide behaviors such as biofilm formation, virulence, and symbiosis. The diazeniumdiolate valdiazen is identified in the opportunistic pathogen Burkholderia cenocepacia H111 as a novel quorum‐sensing signal, yet its protein interactome remains unexplored. In this study, a chemoproteomic pulldown approach is used to identify potential valdiazen‐binding proteins. For these pulldown experiments, a series of alkyne‐linked and biotin‐conjugated valdiazen probes are synthesized. Affinity‐based pulldown experiments using biotin‐valdiazen conjugates successfully identify several putative proteins including an ATP synthase subunit, a succinylglutamate desuccinylase/aspartoacylase, a granule‐associated protein, an acetyl‐CoA hydrolase, a serine protease and an OmpA/MotB precursor. Overall, this study provides insights into the valdiazen–protein interactome in Burkholderia cenocepacia H111, advancing our understanding of the role of valdiazen in bacterial QS.