Abstract
Δlac-Acetogenins are a novel type of inhibitor acting at the terminal electron transfer step of mitochondrial NADH-ubiquinone oxidoreductase (complex I). To identify the binding site of Δlac-acetogenins by photoaffinity labeling, we synthesized a photolabile Δlac-acetogenin that possesses a biotin probe to enable the detection and the isolation of the labeled peptide without the use of a radioisotope. The photolabile Δlac-acetogenin synthesized in this study elicited potent inhibition of bovine heart mitochondrial complex I at the nanomolar level. © Pesticide Science Society of Japan
