Early modification of cytochrome c by hydrogen peroxide triggers its fast degradation

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F21%3A00548122" target="_blank" >RIV/61388971:_____/21:00548122 - isvavai.cz</a>

Alternative codes found

RIV/00216224:14740/21:00124512

Result on the web

<a href="https://www.sciencedirect.com/science/article/pii/S0141813021002373?via%3Dihub" target="_blank" >https://www.sciencedirect.com/science/article/pii/S0141813021002373?via%3Dihub</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.ijbiomac.2021.01.189" target="_blank" >10.1016/j.ijbiomac.2021.01.189</a>

Result language

angličtina

Original language name

Early modification of cytochrome c by hydrogen peroxide triggers its fast degradation

Original language description

Cytochrome c (cyt c), in addition to its function as an electron shuttle in respiratory chain, is able to perform as a pseudo-peroxidase with a critical role during apoptosis. Incubation of cyt c with an excess of hydrogen peroxide leads to a suicide inactivation of the protein, which is accompanied by heme destruction and covalent modification of numerous amino add residues. Although steady-state reactions of cyt c with an excess of hydrogen peroxide represent non-physiological conditions, they might be used for analysis of the first-modified amino add in in vivo. Here, we observed oxidation of tyrosine residues 67 and 74 and heme as the first modifications found upon incubation with hydrogen peroxide. The positions of the oxidized tyrosines suggest a possible migration pathway of hydrogen peroxide-induced radicals from the site of heme localization to the protein surface. Analysis of a size of folded fraction of cyt c upon limited incubation with hydrogen peroxide indicates that the early oxidation of amino acids triggers an accelerated destruction of cyt c. Position of channels from molecular dynamics simulation structures of cyt c points to a location of amino acid residues exposed to reactive oxidants that are thus more prone to covalent modification. (C) 2021 Elsevier B.V. All rights reserved.

Czech name

—

Czech description

—

Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

—

OECD FORD branch

10608 - Biochemistry and molecular biology

Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year

2021

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

International Journal of Biological Macromolecules

ISSN

0141-8130

e-ISSN

1879-0003

Volume of the periodical

174

Issue of the periodical within the volume

MAR 31 2021

Country of publishing house

NL - THE KINGDOM OF THE NETHERLANDS

Number of pages

11

Pages from-to

413-423

UT code for WoS article

000625633200042

EID of the result in the Scopus database

2-s2.0-85100412708