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Area of Science:

  • Biocatalysis and Protein Engineering
  • Synthetic Chemistry and Organometallics

Background:

  • Random mutagenesis offers a pathway to optimize enzyme catalysts without detailed structural information.
  • Integrating synthetic metal cofactors into enzymes (ArMs) presents challenges in expression, screening, and eliminating free cofactor activity.

Purpose of the Study:

  • To establish an efficient platform for creating and screening artificial metalloenzyme libraries via random mutagenesis.
  • To evolve highly selective dirhodium-based cyclopropanase catalysts using this novel platform.

Main Methods:

  • Employed error-prone PCR and combinatorial codon mutagenesis for multiplexed analysis of random mutations.
  • Screened libraries for variants with enhanced selectivity in dirhodium-catalyzed cyclopropanation reactions.
  • Investigated mutations at both active and distal sites within the artificial metalloenzyme.

Main Results:

  • Identified variants with significantly improved enantioselectivity for cyclopropane product formation.
  • Achieved higher catalytic activity compared to previously reported artificial metalloenzyme cyclopropanases.
  • Demonstrated that evolved ArMs for one reaction can be repurposed for other transformations (N-H, S-H, Si-H insertion).

Conclusions:

  • The developed random mutagenesis platform is effective for evolving artificial metalloenzymes with enhanced selectivity and activity.
  • This approach facilitates the discovery of improved biocatalysts for challenging chemical transformations.
  • Artificial metalloenzymes evolved for specific reactions can serve as versatile scaffolds for developing new catalytic functions.