P450 BM3 crystal structures reveal the role of the charged surface residue Lys/Arg184 in inversion of enantioselective styrene epoxidation

Chem Commun (Camb). 2013 May 21;49(41):4694-6. doi: 10.1039/c3cc39076d. Epub 2013 Apr 15.


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

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry
  • Bacterial Proteins / metabolism*
  • Binding Sites
  • Crystallography, X-Ray
  • Cytochrome P-450 Enzyme System / chemistry
  • Cytochrome P-450 Enzyme System / metabolism*
  • Epoxy Compounds / chemistry*
  • NADPH-Ferrihemoprotein Reductase / chemistry
  • NADPH-Ferrihemoprotein Reductase / metabolism*
  • Protein Structure, Tertiary
  • Stereoisomerism
  • Styrene / chemistry*
  • Styrene / metabolism
  • Substrate Specificity


  • Bacterial Proteins
  • Epoxy Compounds
  • Styrene
  • Cytochrome P-450 Enzyme System
  • NADPH-Ferrihemoprotein Reductase
  • flavocytochrome P450 BM3 monoxygenases