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Electron transfer in polysaccharide monooxygenase catalysis.

Richard I Sayler1, William C Thomas1, Alexander J Rose2

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Polysaccharide monooxygenases (PMOs) use redox-active residues for electron transfer, crucial for oxygen activation. This study reveals distinct electron delivery mechanisms for oxygen versus hydrogen peroxide in PMO catalysis.

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Area of Science:

  • Biochemistry and Molecular Biology
  • Enzymology
  • Computational Chemistry

Background:

  • Polysaccharide monooxygenases (PMOs) catalyze challenging C-H bond hydroxylations in carbohydrates.
  • PMO catalysis requires electron transfer and utilizes oxygen (O2) or hydrogen peroxide (H2O2) as cosubstrates.
  • Key questions involve regulating electron delivery to the copper active site and differences between O2 and H2O2 utilization.

Purpose of the Study:

  • To investigate electron transfer pathways in a Myceliophthora thermophila PMO (MtPMO9E).
  • To understand the role of specific residues (Y62, Y168) in electron transfer and O2/H2O2 activation.
  • To elucidate the mechanistic differences in catalysis using O2 versus H2O2.

Main Methods:

  • Computational modeling to identify potential electron transfer pathways.
  • Site-directed mutagenesis (Y62F, Y62W, Y168F) and enzymatic activity assays.
  • X-ray crystallography to determine the structures of wild-type and variant MtPMO9E.
  • Bioinformatic analysis of conserved residues in the AA9 PMO family.

Main Results:

  • Mutation Y62F reduced O2 activity but retained H2O2 activity, highlighting Y62's role in O2 activation.
  • Crystal structures revealed structural effects of Y62 and Y168 mutations.
  • The Y62W variant restored O2 activity, and bioinformatic analysis showed Y/W conservation at position 62 in AA9 PMOs.
  • Redox-active residues appear crucial for electron supply in O2-dependent catalysis across the AA9 family.

Conclusions:

  • Redox-active residues are likely widespread for electron supply in O2-dependent AA9 PMO catalysis.
  • Distinct molecular mechanisms govern PMO catalysis with O2 compared to H2O2.
  • The study provides a framework for understanding substrate-specific electron transfer in PMO enzymes.