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 language | English |
|---|---|
| Pages (from-to) | 156-160 |
| Number of pages | 5 |
| Journal | Biochemical Engineering Journal |
| Volume | 28 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - Feb 15 2006 |
| Externally published | Yes |
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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 journal › Article
}
TY - JOUR
T1 - Peroxidative catalytic behavior of cytochrome c solubilized in reverse micelles
AU - Ono, Tsutomu
AU - Goto, Masahiro
PY - 2006/2/15
Y1 - 2006/2/15
N2 - 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.
AB - 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.
KW - Microemulsion
KW - Oxidation
KW - Peroxidase
KW - Surfactant
UR - http://www.scopus.com/inward/record.url?scp=31944442702&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=31944442702&partnerID=8YFLogxK
U2 - 10.1016/j.bej.2005.10.005
DO - 10.1016/j.bej.2005.10.005
M3 - Article
AN - SCOPUS:31944442702
VL - 28
SP - 156
EP - 160
JO - Biochemical Engineering Journal
JF - Biochemical Engineering Journal
SN - 1369-703X
IS - 2
ER -