Abstract
Cytochrome c solubilized in reversed micelles formulated with di-2-ethylhexyl sulfosuccinate (AOT) has allowed to catalyze the oxidation of o-phenylenediamine (o-PDA) with hydrogen peroxide. The oxidative reaction did not occur effectively by cytochrome c in water. The nanostructural environment in reversed micelles seemed to perturb the three-dimensional structure of the active site of cytochrome c. The product obtained in reversed micelles had a specific absorption spectrum with the absorption peak at 720 nm, indicating a blue-colored solution, whereas common peroxidases such as horseradish peroxidase provided a yellow-colored product in water with the absorption peak at 420 nm. The difference in the oxidative products suggests that AOT molecules play an important role in the specificity of o-PDA oxidation. The dependency of the product species on the pH of the inner droplet in reversed micelles indicated that the specific oxidative product was prepared by electrostatic interaction with AOT molecules.
| Original language | English |
|---|---|
| Pages (from-to) | 955-959 |
| Number of pages | 5 |
| Journal | Journal of Molecular Catalysis B: Enzymatic |
| Volume | 11 |
| Issue number | 4-6 |
| DOIs | |
| Publication status | Published - Jan 22 2001 |
| Externally published | Yes |
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Keywords
- Cytochrome c
- Oxidation
- Peroxidase
- Phenylenediamine
- Reversed micelles
ASJC Scopus subject areas
- Biochemistry
- Catalysis
- Process Chemistry and Technology
Cite this
Catalytic oxidation of o-phenylenediamine by cytochrome c encapsulated in reversed micelles. / Ono, Tsutomu; Kawakami, Koei; Goto, Masahiro; Furusaki, Shintaro.
In: Journal of Molecular Catalysis B: Enzymatic, Vol. 11, No. 4-6, 22.01.2001, p. 955-959.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Catalytic oxidation of o-phenylenediamine by cytochrome c encapsulated in reversed micelles
AU - Ono, Tsutomu
AU - Kawakami, Koei
AU - Goto, Masahiro
AU - Furusaki, Shintaro
PY - 2001/1/22
Y1 - 2001/1/22
N2 - Cytochrome c solubilized in reversed micelles formulated with di-2-ethylhexyl sulfosuccinate (AOT) has allowed to catalyze the oxidation of o-phenylenediamine (o-PDA) with hydrogen peroxide. The oxidative reaction did not occur effectively by cytochrome c in water. The nanostructural environment in reversed micelles seemed to perturb the three-dimensional structure of the active site of cytochrome c. The product obtained in reversed micelles had a specific absorption spectrum with the absorption peak at 720 nm, indicating a blue-colored solution, whereas common peroxidases such as horseradish peroxidase provided a yellow-colored product in water with the absorption peak at 420 nm. The difference in the oxidative products suggests that AOT molecules play an important role in the specificity of o-PDA oxidation. The dependency of the product species on the pH of the inner droplet in reversed micelles indicated that the specific oxidative product was prepared by electrostatic interaction with AOT molecules.
AB - Cytochrome c solubilized in reversed micelles formulated with di-2-ethylhexyl sulfosuccinate (AOT) has allowed to catalyze the oxidation of o-phenylenediamine (o-PDA) with hydrogen peroxide. The oxidative reaction did not occur effectively by cytochrome c in water. The nanostructural environment in reversed micelles seemed to perturb the three-dimensional structure of the active site of cytochrome c. The product obtained in reversed micelles had a specific absorption spectrum with the absorption peak at 720 nm, indicating a blue-colored solution, whereas common peroxidases such as horseradish peroxidase provided a yellow-colored product in water with the absorption peak at 420 nm. The difference in the oxidative products suggests that AOT molecules play an important role in the specificity of o-PDA oxidation. The dependency of the product species on the pH of the inner droplet in reversed micelles indicated that the specific oxidative product was prepared by electrostatic interaction with AOT molecules.
KW - Cytochrome c
KW - Oxidation
KW - Peroxidase
KW - Phenylenediamine
KW - Reversed micelles
UR - http://www.scopus.com/inward/record.url?scp=0035931485&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0035931485&partnerID=8YFLogxK
U2 - 10.1016/S1381-1177(00)00173-9
DO - 10.1016/S1381-1177(00)00173-9
M3 - Article
AN - SCOPUS:0035931485
VL - 11
SP - 955
EP - 959
JO - Journal of Molecular Catalysis - B Enzymatic
JF - Journal of Molecular Catalysis - B Enzymatic
SN - 1381-1177
IS - 4-6
ER -