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Structural basis for selectivity in flavin-dependent monooxygenase-catalyzed oxidative dearomatization.

Attabey Rodríguez Benítez1, Sara Tweedy1, Summer A Baker Dockrey2

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Summary

This study reveals how the enzyme TropB binds substrates, explaining its high selectivity in asymmetric oxidative dearomatization reactions. This structural insight aids future enzyme engineering for synthetic chemistry.

Keywords:
Biocatalysisenantioselective hydroxylationflavin-dependent monooxygenasemolecular dynamicsoxidative dearomatization

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Area of Science:

  • Biocatalysis and Synthetic Chemistry
  • Enzyme Structure and Function
  • Protein Engineering

Background:

  • Biocatalytic reactions offer advantages like selectivity and mild conditions for chemical synthesis.
  • Enzyme substrate scope and selectivity often present a trade-off, limiting their synthetic applications.
  • The flavin-dependent monooxygenase TropB exhibits high selectivity across diverse substrates.

Purpose of the Study:

  • To elucidate the structural basis of substrate binding in TropB.
  • To understand the mechanism behind TropB's high site- and stereoselectivity in asymmetric oxidative dearomatization.
  • To provide a foundation for future protein engineering and reaction development.

Main Methods:

  • X-ray crystallography of TropB.
  • Molecular dynamics (MD) simulations.
  • Quantum mechanics/molecular mechanics (QM/MM) simulations.
  • Experimental validation of binding and catalytic roles.

Main Results:

  • The crystal structure and simulations reveal substrate binding in the phenolate form, unlike canonical Class A FAD-dependent monooxygenases.
  • Two key residues, Arg206 and Tyr239, control substrate positioning through phenolate oxygen binding.
  • Arg206 plays a role in flavin cofactor reduction and dynamics.
  • QM/MM simulations identified interactions governing facial selectivity for enantioselective transformation.

Conclusions:

  • The structural basis for TropB's exceptional site- and stereoselectivity has been elucidated.
  • Understanding TropB's unique substrate binding mechanism opens avenues for enzyme engineering.
  • This work supports the development of novel biocatalysts for complex chemical synthesis.