Peroxidative catalytic behavior of cytochrome c solubilized in reverse micelles

Tsutomu Ono, Masahiro Goto

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

Solubilization of horse heart cytochrome c into reverse micelles, a self-assembled nanostructure composed of sodium di-2-ethylhexyl sulfosuccinate (AOT), enhances the peroxidase activity in the presence of hydrogen peroxide. The catalytic activity of cytochrome c hosted in reverse micellar solution is 10-fold higher than that in water, and which depends on Wo, a molar ratio of water to AOT, and pH in aqueous droplets. In addition, the fluorescence intensity based on the tryptophan residue and the visible absorption identifying the axial Met 80-Fe bond imply that the reverse micellar solubilization induces the cleavage of the heme crevice and thus enables the formation of peroxidase-like peroxide-heme complexes. These results suggest that cytochrome c solubilized in reverse micelles provides a homogeneous catalyst as peroxidase available in organic media.

Original languageEnglish
Pages (from-to)156-160
Number of pages5
JournalBiochemical Engineering Journal
Volume28
Issue number2
DOIs
Publication statusPublished - Feb 15 2006
Externally publishedYes

Fingerprint

Micelles
Cytochromes c
Peroxidase
Proteins
Heme
Water
Nanostructures
Peroxides
Hydrogen peroxide
Tryptophan
Hydrogen Peroxide
Horses
Catalyst activity
Fluorescence
Sodium
Catalysts

Keywords

  • Microemulsion
  • Oxidation
  • Peroxidase
  • Surfactant

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Chemical Engineering(all)

Cite this

Peroxidative catalytic behavior of cytochrome c solubilized in reverse micelles. / Ono, Tsutomu; Goto, Masahiro.

In: Biochemical Engineering Journal, Vol. 28, No. 2, 15.02.2006, p. 156-160.

Research output: Contribution to journalArticle

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