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Cytochrome c peroxidase activity of heme bound amyloid β peptides

Authors :
Somdatta Ghosh Dey
Chandradeep Ghosh
Manas Seal
Olivia Basu
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.

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