Abstract
Solved crystal structures of P450 BM3 variants in complex with styrene provide on the molecular level a first explanation of how a positively charged surface residue inverts the enantiopreference of styrene epoxidation. The obtained insights into productive and non-productive styrene binding modes deepened our understanding of enantioselective epoxidation with P450 BM3.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Bacterial Proteins / chemistry
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Bacterial Proteins / metabolism*
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Binding Sites
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Crystallography, X-Ray
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Cytochrome P-450 Enzyme System / chemistry
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Cytochrome P-450 Enzyme System / metabolism*
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Epoxy Compounds / chemistry*
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NADPH-Ferrihemoprotein Reductase / chemistry
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NADPH-Ferrihemoprotein Reductase / metabolism*
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Protein Structure, Tertiary
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Stereoisomerism
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Styrene / chemistry*
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Styrene / metabolism
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Substrate Specificity
Substances
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Bacterial Proteins
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Epoxy Compounds
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Styrene
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Cytochrome P-450 Enzyme System
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NADPH-Ferrihemoprotein Reductase
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flavocytochrome P450 BM3 monoxygenases