Unprecedented olefin-dependent histidine-kinase inhibitory of zerumbone ring-opening material.

Abstract Zerumbone ring-opening derivative, 4 (10 E /10 Z  = 3/2), inhibited autophosphorylation of the essential histidine–kinase YycG existing in Bacillus subtilis constituting a two-component system (TCS). Generation of 4 E -form could be regulated chemically using the difference from the ring-opening reactivity of the precursor forming of 4 and pure 4 E was isolated. The stereoisomer, 4 E , showed main inhibition activity of autophosphorylation of YycG (IC 50  = 63.5 μM).