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pubmed-article:11718725pubmed:abstractTextWe report here oxidation of propylbenzene and 3-chlorostyrene by wild-type cytochrome P450 BM-3 with high turnover (479 nmol 1-phenyl-1-propanol/min/nmol P450 and 300 nmol 3-chlorostyrene oxide/min/nmol P450). Furthermore, the residue size at position 87 of P450 BM-3 was found to play critical roles in determining stereoselectivity in oxidation of propylbenzene and 3-chlorostyrene. Replacement of Phe87 with Val, Ala and Gly resulted in decreases in optical purity of produced (R)-(+)-1-phenyl-1-propanol from 90.0 to 37.4, 26.0 and -15.6% e.e., respectively, and in increases in those of produced (R)-(+)-3-chlorostyrene oxide from -61.0 to -38.0, 67.0 and 94.6% e.e., respectively.lld:pubmed
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pubmed-article:11718725pubmed:dateRevised2008-11-21lld:pubmed
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pubmed-article:11718725pubmed:articleTitleResidue size at position 87 of cytochrome P450 BM-3 determines its stereoselectivity in propylbenzene and 3-chlorostyrene oxidation.lld:pubmed
pubmed-article:11718725pubmed:affiliationDivision of Applied Life Science, Graduate School of Agriculture, Kyoto University, Japan.lld:pubmed
pubmed-article:11718725pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:11718725pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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