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.
TY - JOUR
AU - Bolic, Bojana
AU - Mijuskovic, Ana
AU - Popovic-Bijelic, Ana
AU - Nikolić-Kokić, Aleksandra
AU - Spasić, Snežana
AU - Blagojevic, Dusko
AU - Spasić, Mihajlo
AU - Spasojević, Ivan
PY - 2015
UR - https://cer.ihtm.bg.ac.rs/handle/123456789/1787
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
VL - 51
SP - 19
EP - 23
DO - 10.1016/j.niox.2015.09.008
UR - Conv_3454
ER -
@article{
author = "Bolic, Bojana and Mijuskovic, Ana and Popovic-Bijelic, Ana and Nikolić-Kokić, Aleksandra and Spasić, Snežana and Blagojevic, Dusko 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",
volume = "51",
pages = "19-23",
doi = "10.1016/j.niox.2015.09.008",
url = "Conv_3454"
}
Bolic, B., Mijuskovic, A., Popovic-Bijelic, A., Nikolić-Kokić, A., Spasić, S., Blagojevic, 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_3454
Bolic B, Mijuskovic A, Popovic-Bijelic A, Nikolić-Kokić A, Spasić S, Blagojevic 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
Conv_3454 .
Bolic, Bojana, Mijuskovic, Ana, Popovic-Bijelic, Ana, Nikolić-Kokić, Aleksandra, Spasić, Snežana, Blagojevic, Dusko, 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 .,
Conv_3454 .
