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Functionally Distinct Bacterial Cytochrome c Peroxidases Proceed through a Common (Electro)catalytic Intermediate.

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The study reveals a key catalytic intermediate in bacterial diheme cytochrome c peroxidase (So CcP) activation. This finding, observed via protein film voltammetry, clarifies the enzyme

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Area of Science:

  • Biochemistry and enzymology
  • Bioinorganic chemistry
  • Protein electrochemistry

Background:

  • Diheme cytochrome c peroxidases (bCcPs) are crucial enzymes involved in peroxide metabolism.
  • The bacterial bCcP from Shewanella oneidensis (So CcP) requires reductive activation to become catalytically competent.
  • Understanding the mechanism of So CcP is essential for elucidating peroxide detoxification pathways.

Purpose of the Study:

  • To investigate the mechanism of hydrogen peroxide turnover by the reductively activated So CcP.
  • To identify and characterize on-pathway catalytic intermediates in So CcP.
  • To compare the catalytic mechanism of So CcP with constitutively active bCcPs like Ne CcP.

Main Methods:

  • Protein film voltammetry was employed to study So CcP electrochemistry and catalysis.
  • Enzyme activation was achieved using sodium l-ascorbate.
  • Site-directed mutagenesis was used to probe the role of active site residues and surface loops.

Main Results:

  • A highly active catalytic intermediate was observed for So CcP in a high potential regime.
  • The rate-limiting step involves a proton-coupled single electron reduction of a high valent iron species.
  • Mutational analysis confirmed the involvement of a surface loop (loop 1) and His81 in the reductive activation process.

Conclusions:

  • This study provides the first observation of an on-pathway catalytic intermediate for a reductively activated bacterial bCcP.
  • Unexpected mechanistic similarities exist between reductively activated (So CcP) and constitutively active (Ne CcP) bCcPs.
  • The findings highlight conserved features in the rate-limiting steps across different classes of bCcPs.