Abstract
Abstract Mutations of myoglobin reconstituted with Mn porphycene (rMb) were investigated to enhance the enantioselectivity for hydroxylation of ethylbenzene. The 21 mutants of rMb predicted by models using molecular dynamics simulation were prepared. Several rMb mutants enhance the enantiomeric excess (ee) values up to 69% and 57% for (S)- and (R)-1-phenylethanols, respectively, compared with wild-type rMb (17% ee for (S)-1-phenylethanol). Furthermore, the crystal structures demonstrate slightly expanded spaces to support the substrate binding behavior indicated in the simulation.
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