@article{oai:nagoya.repo.nii.ac.jp:00025139,
 author = {Suzuki, Kazuto and Kyle, Stanfield  Joshua and Shoji, Osami and Yanagisawa, Sota and Sugimoto, Hiroshi and Shiro, Yoshitsugu and Watanabe, Yoshihito},
 journal = {Catalysis Science and Technology},
 month = {Aug},
 note = {The hydroxylation of non-native substrates catalysed by wild-type P450BM3 is reported, wherein “decoy molecules”, i.e., native substrate mimics, controlled the stereoselectivity of hydroxylation reactions. We employed decoy molecules with diverse structures, resulting in either a significant improvement in enantioselectivity or clear inversion of stereoselectivity in the benzylic hydroxylation of alkylbenzenes and cycloalkylbenzenes. For example, supplementation of wild-type P450BM3 with 5-cyclohexylvaleric acid-L-phenylalanine (5CHVA-Phe) and Z-proline-L-phenylalanine yielded 53% (R) ee and 56% (S) ee for indane hydroxylation, respectively, although 16% (S) ee was still observed in the absence of any additives. Moreover, we performed a successful crystal structure analysis of 5CHVA-L-tryptophan-bound P450BM3 at 2.00 Å, which suggests that the changes in selectivity observed were caused by conformational changes in the enzyme induced by binding of the decoy molecules.},
 pages = {3332--3338},
 title = {Control of stereoselectivity of benzylic hydroxylation catalysed by wild-type cytochrome P450BM3 using decoy molecules},
 volume = {7},
 year = {2017}
}