摘要：Cytochrome P450 OleT_(SA),a new cytochrome P450 enzyme from Staphylococcus aureus,catalyzes the oxidative decarboxylation and hydroxylation of fatty acids to generate terminal alkenes and fatty *** mechanism of this bifurcative chemistry remains largely ***,a class of derivatized fatty acids were synthesized as probes to investigate the effects of substrate structure on the product type of P450 OleT_(SA).The results demonstrate that the fine-tuned structure of substrates,even in a remote distance from the carboxyl group,significantly regulates OleT catalyzed decarboxylation/hydroxylation *** docking analysis indicated the potential interactions between the carboxylate groups of different probes and the enzyme active center which was attributed to the bifurcative chemistry.