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A Well-Defined Osmium-Cupin Complex: Hyperstable Artificial Osmium Peroxygenase.

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A Thermotoga maritima protein (TM1459) was engineered into a robust osmium peroxygenase. This artificial enzyme efficiently catalyzes alkene dihydroxylation, showing enhanced activity and selectivity through protein scaffold modification.

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Area of Science:

  • Biocatalysis and Enzyme Engineering
  • Organometallic Chemistry
  • Protein Chemistry

Background:

  • The development of stable and efficient artificial metalloenzymes is crucial for green chemistry.
  • Repurposing existing proteins offers a sustainable route to novel biocatalysts.
  • Osmium-based catalysts are known for their high activity in oxidation reactions.

Purpose of the Study:

  • To engineer a thermally stable cupin protein (TM1459) into an osmium peroxygenase.
  • To investigate the structural and catalytic properties of the resulting artificial metalloenzyme.
  • To evaluate its efficiency and selectivity in alkene dihydroxylation reactions.

Main Methods:

  • Metal-substitution strategy using osmium (Os) to repurpose TM1459.
  • Spectroscopic analysis and X-ray crystallography to characterize the Os-bound protein.
  • Catalytic evaluation of the Os-TM1459 for alkene cis-dihydroxylation.

Main Results:

  • A robust Os-TM1459 artificial metalloenzyme with high thermal stability (Tm ≈ 120 °C) was created.
  • Two distinct Os coordination geometries (O3N3 and O2N4 donor sets) were identified.
  • The O2N4-bound Os-TM1459 efficiently catalyzed alkene dihydroxylation with high turnover numbers (up to 9100).
  • The protein scaffold demonstrated regioselectivity control and suppressed H2O2 disproportionation.
  • Site-directed mutagenesis enhanced catalytic activity by approximately 3-fold.

Conclusions:

  • Osmium-bound TM1459 functions as an efficient and robust peroxygenase.
  • The protein scaffold plays a critical role in controlling catalytic activity, stability, and selectivity.
  • Os-TM1459 represents an evolvable platform for developing novel osmium-based biocatalysts.