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pubmed-article:12121073pubmed:abstractTextThe H64D/V68A and H64D/V68S mutants of Myoglobin are found to oxidize thioanisole with high enantioselectivity and reactivity. These mutants are also capable of enantioselective binding of alpha-methylbenzylamine, which mimics an expected sulfoxidation intermediate. The kinetic study of the amine binding shows that the Fe-O bond cleavage in the intermediate may be the chiral discrimination step of the sulfoxidation.lld:pubmed
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pubmed-article:12121073pubmed:dateRevised2008-1-17lld:pubmed
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pubmed-article:12121073pubmed:articleTitleAsymmetric sulfoxidation and amine binding by H64D/V68A and H64D/V68S Mb: mechanistic insight into the chiral discrimination step.lld:pubmed
pubmed-article:12121073pubmed:affiliationDepartment of Structural Molecular Science, The Graduate University for Advanced Studies, Okazaki 444-8585, Japan.lld:pubmed
pubmed-article:12121073pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:12121073pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed