RIMSI - Repository of Institute for Multidisciplinary Research
University of Belgrade - Institute for Multidisciplinary Research
    • English
    • Српски
    • Српски (Serbia)
  • English 
    • English
    • Serbian (Cyrillic)
    • Serbian (Latin)
  • Login
View Item 
  •   RIMSI
  • Institut za multidisciplinarna istraživanja
  • Radovi istraživača / Researchers’ publications
  • View Item
  •   RIMSI
  • Institut za multidisciplinarna istraživanja
  • Radovi istraživača / Researchers’ publications
  • View Item
JavaScript is disabled for your browser. Some features of this site may not work without it.

Reactions of superoxide dismutases with HS-/H2S and superoxide radical anion: An in vitro EPR study

Thumbnail
2015
843.pdf (739.7Kb)
Authors
Bolic, Bojana
Mijusković, Ana
Popovic-Bijelic, Ana
Nikolić-Kokić, Aleksandra
Spasic, Snežana
Blagojević, Duško
Spasić, Mihajlo
Spasojević, Ivan
Article (Accepted Version)
Metadata
Show full item record
Abstract
Interactions of hydrogen sulfide (HS-/H2S), a reducing signaling species, with superoxide dimutases (SOD) are poorly understood. We applied low-T EPR spectroscopy to examine the effects of HS-/H2S and superoxide radical anion (O-2(-)) on metallocenters of FeSOD, MnSOD, and CuZnSOD. HS-/H2S did not affect FeSOD, whereas active centers of MnSOD and CuZnSOD were open to this agent. Cu2+ was reduced to Cu1+, while manganese appears to be released from MnSOD active center. Untreated and O-2(-) treated FeSOD and MnSOD predominantly show 5 d-electron systems, i.e. Fe3+ and Mn2+. Our study provides new details on the mechanisms of (patho)physiological effects of HS-/H2S.
Keywords:
Superoxide dismutase / Manganese / Iron / H2S / EPR / Copper
Source:
Nitric Oxide-Biology and Chemistry, 2015, 51, 19-23
Publisher:
  • Academic Press Inc Elsevier Science, San Diego
Funding / projects:
  • Molecular mechanisms of redox signalling in homeostasis: adaptation and pathology (RS-173014)
  • Biomarkers in neurodegenerative and malignant processes (RS-41005)
Note:
  • This is the peered review version of the paper: Bolic, B., Mijusković, A., Popovic-Bijelic, A., Nikolić-Kokić, A., Spasic, S., Blagojević, D., Spasić, M.,& Spasojević, I.. (2015). Reactions of superoxide dismutases with HS-/H2S and superoxide radical anion: An in vitro EPR study. in Nitric Oxide-Biology and Chemistry Academic Press Inc Elsevier Science, San Diego., 51, 19-23. https://doi.org/10.1016/j.niox.2015.09.008 conv_1488

DOI: 10.1016/j.niox.2015.09.008

ISSN: 1089-8603

PubMed: 26436856

WoS: 000366065100003

Scopus: 2-s2.0-84944719548
[ Google Scholar ]
5
4
URI
http://rimsi.imsi.bg.ac.rs/handle/123456789/846
Collections
  • Radovi istraživača / Researchers’ publications
Institution/Community
Institut za multidisciplinarna istraživanja
TY  - JOUR
AU  - Bolic, Bojana
AU  - Mijusković, Ana
AU  - Popovic-Bijelic, Ana
AU  - Nikolić-Kokić, Aleksandra
AU  - Spasic, Snežana
AU  - Blagojević, Duško
AU  - Spasić, Mihajlo
AU  - Spasojević, Ivan
PY  - 2015
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/846
AB  - Interactions of hydrogen sulfide (HS-/H2S), a reducing signaling species, with superoxide dimutases (SOD) are poorly understood. We applied low-T EPR spectroscopy to examine the effects of HS-/H2S and superoxide radical anion (O-2(-)) on metallocenters of FeSOD, MnSOD, and CuZnSOD. HS-/H2S did not affect FeSOD, whereas active centers of MnSOD and CuZnSOD were open to this agent. Cu2+ was reduced to Cu1+, while manganese appears to be released from MnSOD active center. Untreated and O-2(-) treated FeSOD and MnSOD predominantly show 5 d-electron systems, i.e. Fe3+ and Mn2+. Our study provides new details on the mechanisms of (patho)physiological effects of HS-/H2S.
PB  - Academic Press Inc Elsevier Science, San Diego
T2  - Nitric Oxide-Biology and Chemistry
T1  - Reactions of superoxide dismutases with HS-/H2S and superoxide radical anion: An in vitro EPR study
EP  - 23
SP  - 19
VL  - 51
DO  - 10.1016/j.niox.2015.09.008
ER  - 
@article{
author = "Bolic, Bojana and Mijusković, Ana and Popovic-Bijelic, Ana and Nikolić-Kokić, Aleksandra and Spasic, Snežana and Blagojević, Duško and Spasić, Mihajlo and Spasojević, Ivan",
year = "2015",
abstract = "Interactions of hydrogen sulfide (HS-/H2S), a reducing signaling species, with superoxide dimutases (SOD) are poorly understood. We applied low-T EPR spectroscopy to examine the effects of HS-/H2S and superoxide radical anion (O-2(-)) on metallocenters of FeSOD, MnSOD, and CuZnSOD. HS-/H2S did not affect FeSOD, whereas active centers of MnSOD and CuZnSOD were open to this agent. Cu2+ was reduced to Cu1+, while manganese appears to be released from MnSOD active center. Untreated and O-2(-) treated FeSOD and MnSOD predominantly show 5 d-electron systems, i.e. Fe3+ and Mn2+. Our study provides new details on the mechanisms of (patho)physiological effects of HS-/H2S.",
publisher = "Academic Press Inc Elsevier Science, San Diego",
journal = "Nitric Oxide-Biology and Chemistry",
title = "Reactions of superoxide dismutases with HS-/H2S and superoxide radical anion: An in vitro EPR study",
pages = "23-19",
volume = "51",
doi = "10.1016/j.niox.2015.09.008"
}
Bolic, B., Mijusković, A., Popovic-Bijelic, A., Nikolić-Kokić, A., Spasic, S., Blagojević, D., Spasić, M.,& Spasojević, I.. (2015). Reactions of superoxide dismutases with HS-/H2S and superoxide radical anion: An in vitro EPR study. in Nitric Oxide-Biology and Chemistry
Academic Press Inc Elsevier Science, San Diego., 51, 19-23.
https://doi.org/10.1016/j.niox.2015.09.008
Bolic B, Mijusković A, Popovic-Bijelic A, Nikolić-Kokić A, Spasic S, Blagojević D, Spasić M, Spasojević I. Reactions of superoxide dismutases with HS-/H2S and superoxide radical anion: An in vitro EPR study. in Nitric Oxide-Biology and Chemistry. 2015;51:19-23.
doi:10.1016/j.niox.2015.09.008 .
Bolic, Bojana, Mijusković, Ana, Popovic-Bijelic, Ana, Nikolić-Kokić, Aleksandra, Spasic, Snežana, Blagojević, Duško, Spasić, Mihajlo, Spasojević, Ivan, "Reactions of superoxide dismutases with HS-/H2S and superoxide radical anion: An in vitro EPR study" in Nitric Oxide-Biology and Chemistry, 51 (2015):19-23,
https://doi.org/10.1016/j.niox.2015.09.008 . .

DSpace software copyright © 2002-2015  DuraSpace
About RIMSI | Send Feedback

OpenAIRERCUB
 

 

All of DSpaceCommunitiesAuthorsTitlesSubjectsThis institutionAuthorsTitlesSubjects

Statistics

View Usage Statistics

DSpace software copyright © 2002-2015  DuraSpace
About RIMSI | Send Feedback

OpenAIRERCUB