Abstract
The active conformation of antimycin A, a specific inhibitor of mitochondrial complex-III, expected from structure–activity studies is consistent with that come from X-ray crystallography of the enzyme. The structure–activity studies of acetogenins, potent inhibitors of complex-I, indicate that these inhibitors elicit potent activities only when the γ-lactone ring and hydroxylated THF ring moieties are directly linked by an alkyl spacer. Δlac-Acetogenins that are acetogenin mimics possessing two alkyl tails without a γ-lactone ring appeared to be a novel type of complex-I inhibitor, the binding site of which differs from that of ordinary complex-I inhibitors. © Pesticide Science Society of Japan
