title: P450 BM3 crystal structures reveal the role of the charged surface residue Lys/Arg184 in inversion of enantioselective styrene epoxidation.
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.
authors.affiliation: Lehrstuhl für Biotechnologie, RWTH Aachen University, Worringerweg 1, 52074 Aachen, Germany.
authors.forename: Aamir
authors.initials: A
authors.lastname: Shehzad
authors.forename: Saravanan
authors.initials: S
authors.lastname: Panneerselvam
authors.forename: Marina
authors.initials: M
authors.lastname: Linow
authors.forename: Marco
authors.initials: M
authors.lastname: Bocola
authors.forename: Danilo
authors.initials: D
authors.lastname: Roccatano
authors.forename: Jochen
authors.initials: J
authors.lastname: Mueller-Dieckmann
authors.forename: Matthias
authors.initials: M
authors.lastname: Wilmanns
authors.forename: Ulrich
authors.initials: U
authors.lastname: Schwaneberg
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D001665:Binding Sites; D018360:Crystallography, X-Ray; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry / Q000378:metabolism*; D004852:Epoxy Compounds / Q000737:chemistry*; D009251:NADPH-Ferrihemoprotein Reductase / Q000737:chemistry / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D013237:Stereoisomerism; D020058:Styrene / Q000737:chemistry* / Q000378:metabolism; D013379:Substrate Specificity
chemical_list: D001426:Bacterial Proteins; D004852:Epoxy Compounds; D020058:Styrene; D003577:Cytochrome P-450 Enzyme System; D009251:NADPH-Ferrihemoprotein Reductase; C052423:flavocytochrome P450 BM3 monoxygenases