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Structure and function of type I copper in multicopper oxidases.

T Sakurai1, K Kataoka

  • 1Graduate School of Natural Science and Technology, Kanazawa University, Kakuma, Kanazawa, 920-1192, Japan. ts0513@kenroku.kanazawa-u.ac.jp

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Multicopper oxidases feature a type I copper center crucial for electron transfer. Mutations altering its structure, particularly the cysteine ligand, can trap reaction intermediates during dioxygen reduction.

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Area of Science:

  • Biochemistry
  • Protein Chemistry
  • Enzymology

Background:

  • Multicopper oxidases (MCOs) contain a type I copper center with specific coordinating ligands (Cys, His, Met/Phe/Leu).
  • This type I copper center shares spectral similarities with blue copper centers in blue copper proteins.
  • Electron transfer in MCOs involves intricate pathways due to the buried nature of the type I copper center.

Purpose of the Study:

  • To investigate the role of the type I copper center's fourth ligand in electron transfer.
  • To explore how mutations affect intramolecular electron transfer rates.
  • To examine the consequences of cysteine ligand mutation on dioxygen reduction intermediates.

Main Methods:

  • Spectroscopic analysis of the type I copper center.
  • Site-directed mutagenesis of MCOs to alter ligand coordination.
  • Kinetic studies to determine electron transfer rates.
  • Characterization of reaction intermediates during dioxygen reduction.

Main Results:

  • The type I copper center's spectral properties and alkaline transition resemble those of blue copper proteins.
  • Specific pathways, including hydrogen bonds and His-Cys-His sequences, facilitate electron transfer to/from the buried type I copper center.
  • Mutation of the fourth ligand modulates intramolecular electron transfer rates.
  • Cysteine ligand mutation results in a vacant type I copper center and traps reaction intermediates.

Conclusions:

  • The fourth ligand of the type I copper center is a key determinant of electron transfer rates in MCOs.
  • The His-Cys-His sequence is vital for relaying electrons between copper centers.
  • Targeted mutations, especially at the cysteine residue, offer insights into MCO reaction mechanisms and intermediate stabilization.