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Cytochrome c peroxidase activity of heme bound amyloid β peptides
- Source :
- Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry. 21(5-6)
- Publication Year :
- 2016
-
Abstract
- Heme bound amyloid β (Aβ) peptides, which have been associated with Alzheimer's disease (AD), can catalytically oxidize ferrocytochrome c (Cyt c(II)) in the presence of hydrogen peroxide (H2O2). The rate of catalytic oxidation of Cyt(II) c has been found to be dependent on several factors, such as concentration of heme(III)-Aβ, Cyt(II) c, H2O2, pH, ionic strength of the solution, and peptide chain length of Aβ. The above features resemble the naturally occurring enzyme cytochrome c peroxidase (CCP) which is known to catalytically oxidize Cyt(II) c in the presence of H2O2. In the absence of heme(III)-Aβ, the oxidation of Cyt(II) c is not catalytic. Thus, heme-Aβ complex behaves as CCP.
- Subjects :
- Stereochemistry
Peptide
Heme
010402 general chemistry
Spectrum Analysis, Raman
environment and public health
01 natural sciences
Biochemistry
Inorganic Chemistry
chemistry.chemical_compound
Hydrogen peroxide
chemistry.chemical_classification
Amyloid beta-Peptides
biology
010405 organic chemistry
Cytochrome c peroxidase
Cytochrome c
Cytochrome-c peroxidase activity
Hydrogen Peroxide
Cytochrome-c Peroxidase
0104 chemical sciences
enzymes and coenzymes (carbohydrates)
Kinetics
Enzyme
chemistry
Ionic strength
embryonic structures
cardiovascular system
biology.protein
Subjects
Details
- ISSN :
- 14321327
- Volume :
- 21
- Issue :
- 5-6
- Database :
- OpenAIRE
- Journal :
- Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry
- Accession number :
- edsair.doi.dedup.....85e76ca7139d8d5dc11b40ff6e5dc75f