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

J 2021

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

TOMASKOVA, N., P. NOVAK, T. KOZAR, M. PETRENCAKOVA, D. JANCURA et. al.

Basic information

Original name

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

Authors

TOMASKOVA, N., P. NOVAK, T. KOZAR, M. PETRENCAKOVA, D. JANCURA, G. YASSAGHI, P. MAN and E. SEDLAK

Edition

INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES, 2021, 0141-8130

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10608 Biochemistry and molecular biology

Country of publisher

Netherlands

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

URL

Impact factor

Impact factor: 8.025

RIV identification code

RIV/00216224:14740/21:00124512

Organization unit

Central European Institute of Technology

DOI

http://dx.doi.org/10.1016/j.ijbiomac.2021.01.189

UT WoS

000625633200042

Keywords in English

Pseudo-peroxidasesOxidative damageReactive oxygen speciesProtein channelsSuicide inactivation

Abstract

V originále

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.

Links

90127, large research infrastructures

Name: CIISB II

Citovat

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. 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.

@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.

Detailed Information on Publication Record