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Published on: April 11, 2014

Ascorbate peroxidase activity of cytochrome c.

Cristina Bischin1, Florina Deac, Radu Silaghi-Dumitrescu

  • 1Department of Chemistry and Chemical Engineering, 'Babes-Bolyai' University, Cluj-Napoca RO-400028, Romania. cristina_bischin@yahoo.com

Free Radical Research
|December 7, 2010
PubMed
Summary

Cytochrome c's peroxidase activity, enhanced by modifications, catalyzes peroxide consumption by ascorbate. This interaction with a ferryl intermediate may influence cell signaling and damage pathways involving cytochrome c and peroxides.

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Free Radical Chemistry

Background:

  • Cytochrome c exhibits peroxidase-type reactivity, potentially involved in free radical production and apoptosis.
  • Understanding cytochrome c's role in oxidative processes is crucial for cell biology and disease research.

Purpose of the Study:

  • To investigate cytochrome c's catalysis of peroxide consumption by ascorbate.
  • To explore how modifications affecting heme iron accessibility influence this peroxidase activity.
  • To characterize reaction intermediates and their potential biological relevance.

Main Methods:

  • Utilized stopped-flow UV-vis spectroscopy to detect reaction intermediates.
  • Employed chemical modifications (carboxymethylation, cardiolipin addition, guanidinium hydrochloride denaturation) to alter cytochrome c structure.
  • Assayed peroxide consumption by ascorbate in the presence of modified cytochrome c.

Main Results:

  • Cytochrome c efficiently catalyzes peroxide consumption by ascorbate.
  • Peroxidase activity is significantly enhanced when the heme iron's sixth coordination position is more accessible.
  • A ferryl species, similar to globin Compound II, was detected as a reaction intermediate.
  • Physiological ascorbate concentrations interact with this ferryl intermediate.

Conclusions:

  • Modified cytochrome c exhibits enhanced peroxidase activity, facilitating peroxide breakdown by ascorbate.
  • The formation of a ferryl intermediate is key to this catalytic process.
  • The interaction of ascorbate with the ferryl species has potential implications for cellular signaling and damage mechanisms involving cytochrome c and peroxides.