Other formats:
BibTeX
LaTeX
RIS
@article{1846467,
author = {Tomaskova, N. and Novak, P. and Kozar, T. and Petrencakova, M. and Jancura, D. and Yassaghi, G. and Man, P. and Sedlak, E.},
article_number = {MAR},
doi = {http://dx.doi.org/10.1016/j.ijbiomac.2021.01.189},
keywords = {Pseudo-peroxidasesOxidative damageReactive oxygen speciesProtein channelsSuicide inactivation},
language = {eng},
issn = {0141-8130},
journal = {INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES},
title = {Early modification of cytochrome c by hydrogen peroxide triggers its fast degradation},
url = {https://www.sciencedirect.com/science/article/pii/S0141813021002373?via%3Dihub},
volume = {174},
year = {2021}
}
TY - JOUR
ID - 1846467
AU - Tomaskova, N. - Novak, P. - Kozar, T. - Petrencakova, M. - Jancura, D. - Yassaghi, G. - Man, P. - Sedlak, E.
PY - 2021
TI - Early modification of cytochrome c by hydrogen peroxide triggers its fast degradation
JF - INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
VL - 174
IS - MAR
SP - 413-423
EP - 413-423
SN - 01418130
KW - Pseudo-peroxidasesOxidative damageReactive oxygen speciesProtein channelsSuicide inactivation
UR - https://www.sciencedirect.com/science/article/pii/S0141813021002373?via%3Dihub
N2 - 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.
ER -
TOMASKOVA, N., P. NOVAK, T. KOZAR, M. PETRENCAKOVA, D. JANCURA, G. YASSAGHI, P. MAN and E. SEDLAK. Early modification of cytochrome c by hydrogen peroxide triggers its fast degradation. \textit{INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES}. 2021, vol.~174, MAR, p.~413-423. ISSN~0141-8130. Available from: https://dx.doi.org/10.1016/j.ijbiomac.2021.01.189.
|
