Year: 2004
Type: article
Abstract: The peroxidase activity of cytochrome c was studied by using a chromogen, 2,2'-azinobis-(2-ethylbenzthiazoline-6-sulfonate) (ABTS). Initial rate of ABTS oxidation formation was linear with respect to the concentration of cytochrome c between 2.5-10 ${\mu}$ M and $H_2O_2$ between 0.1-0.5 mM. The optimal pH for the peroxidase activity of cytochrome c was 7.0-8.5. The peroxidase activity retained about 40% of the maximum activity when exposed at 60 $^{\circ}C$ . for 10 min. The peroxidase activity showed a typical Michaelis-Menten kinetics for $H_2O_2$ which Km value was 29.6 mM. Radical scavengers inhibited the peroxidase activity of cytochrome c. The peroxidase activity was significantly inhibited by the low concentration of iron chelator, deferoxamine. The results suggested that the peroxidase activity was associated with iron in the heme of cytochrome c.
Author: Kim, Nam-Hoon;Jeong, Moon-Sik;Choi, Soo-Young;Kang, Jung-Hoon;
Institutions: Hallym University, Cheongju University
Language: English
Subfield: Inorganic Chemistry
Field: Chemistry
Domain: Physical Sciences
Open Access status: bronze
OpenAlex ID: W2150406927