TY  - JOUR
AU  - Filipović, Miloš R.
AU  - Stanić-Vučinić, Dragana
AU  - Raičević, Smiljana
AU  - Spasić, Mihajlo B.
AU  - Niketić, Vesna
PY  - 2007
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/4335
AB  - The present study demonstrates that manganese superoxide dismutase (MnSOD) Escherichia coli, binds nitric oxide (NO) and stimulates its decay under both anaerobic and aerobic conditions. The results indicate that previously observed MnSOD-catalyzed NO disproportionation (dismutation) into nitrosonium (NO + ) and nitroxyl (NO - ) species under anaerobic conditions is also operative in the presence of molecular oxygen. Upon sustained aerobic exposure to NO, MnSOD-derived NO - species initiate the formation of peroxynitrite (ONOO - ) leading to enzyme tyrosine nitration, oxidation and (partial) inactivation. The results suggest that both ONOO - decomposition and ONOO - -dependent tyrosine residue nitration and oxidation are enhanced by metal centre-mediated catalysis. We show that the generation of ONOO - is accompanied by the formation of substantial amounts of H 2 O 2 . MnSOD is a critical mitochondrial antioxidant enzyme, which has been found to undergo tyrosine nitration and inactivation in various pathologies associated with the overproduction of NO. The results of the present study can account for the molecular specificity of MnSOD nitration in vivo. The interaction of NO with MnSOD may represent a novel mechanism by which MnSOD protects the cell from deleterious effects associated with overproduction of NO.
PB  - USA :Taylor & Francis INC
T2  - Free Radical Research
T1  - Consequences of MnSOD interactions with nitric oxide: Nitric oxide dismutation and the generation of peroxynitrite and hydrogen peroxide
VL  - 41
IS  - 1
SP  - 62
EP  - 72
DO  - 10.1080/10715760600944296
ER  - 

@article{
author = "Filipović, Miloš R. and Stanić-Vučinić, Dragana and Raičević, Smiljana and Spasić, Mihajlo B. and Niketić, Vesna",
year = "2007",
abstract = "The present study demonstrates that manganese superoxide dismutase (MnSOD) Escherichia coli, binds nitric oxide (NO) and stimulates its decay under both anaerobic and aerobic conditions. The results indicate that previously observed MnSOD-catalyzed NO disproportionation (dismutation) into nitrosonium (NO + ) and nitroxyl (NO - ) species under anaerobic conditions is also operative in the presence of molecular oxygen. Upon sustained aerobic exposure to NO, MnSOD-derived NO - species initiate the formation of peroxynitrite (ONOO - ) leading to enzyme tyrosine nitration, oxidation and (partial) inactivation. The results suggest that both ONOO - decomposition and ONOO - -dependent tyrosine residue nitration and oxidation are enhanced by metal centre-mediated catalysis. We show that the generation of ONOO - is accompanied by the formation of substantial amounts of H 2 O 2 . MnSOD is a critical mitochondrial antioxidant enzyme, which has been found to undergo tyrosine nitration and inactivation in various pathologies associated with the overproduction of NO. The results of the present study can account for the molecular specificity of MnSOD nitration in vivo. The interaction of NO with MnSOD may represent a novel mechanism by which MnSOD protects the cell from deleterious effects associated with overproduction of NO.",
publisher = "USA :Taylor & Francis INC",
journal = "Free Radical Research",
title = "Consequences of MnSOD interactions with nitric oxide: Nitric oxide dismutation and the generation of peroxynitrite and hydrogen peroxide",
volume = "41",
number = "1",
pages = "62-72",
doi = "10.1080/10715760600944296"
}

Filipović, M. R., Stanić-Vučinić, D., Raičević, S., Spasić, M. B.,& Niketić, V.. (2007). Consequences of MnSOD interactions with nitric oxide: Nitric oxide dismutation and the generation of peroxynitrite and hydrogen peroxide. in Free Radical Research
USA :Taylor & Francis INC., 41(1), 62-72.
https://doi.org/10.1080/10715760600944296

Filipović MR, Stanić-Vučinić D, Raičević S, Spasić MB, Niketić V. Consequences of MnSOD interactions with nitric oxide: Nitric oxide dismutation and the generation of peroxynitrite and hydrogen peroxide. in Free Radical Research. 2007;41(1):62-72.
doi:10.1080/10715760600944296 .

Filipović, Miloš R., Stanić-Vučinić, Dragana, Raičević, Smiljana, Spasić, Mihajlo B., Niketić, Vesna, "Consequences of MnSOD interactions with nitric oxide: Nitric oxide dismutation and the generation of peroxynitrite and hydrogen peroxide" in Free Radical Research, 41, no. 1 (2007):62-72,
https://doi.org/10.1080/10715760600944296 . .

TY  - CHAP
AU  - Filipović, Miloš
AU  - Stanić, Dragana
AU  - Nikolić, Milan
AU  - Stojanović, Srđan
AU  - Raičević, Smiljana
AU  - Niketić, Vesna
PY  - 2005
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6509
AB  - In vitro studies demonstrated that peroxynitrite inactivates both human
recombinant MnSOD (hrMnSOD) and E. coli MnSOD causing enzyme tyrosine
residue(s) nitration. This led to a suggestion that human MnSOD nitration and
inactivation in vivo, detected in various deseases associated with oxidative stress and
overproduction of nitric monoxide (NO)–conditions that favor peroxynitrite
formation–are also caused by peroxynitrite. In a previous study we demonstrated
that the exposure of E. coli MnSOD to NO under the anaerobic conditions causes
NO conversion (dismutation) into reactive nitrosonium (NO
+
) and nitroxyl
(HNO/NO
–
) species, which produce enzyme modifications and inactivation (Niketic
et al., Free Rad. Biol. Med. 27: 992 (1999)). The present study shows that interaction
of NO with E. coli MnSOD leads to the formation of nitrating species capable
of nitrating and oxidizing enzyme tyrosine residues, as well as that these species
are less invasive than peroxynitrite in producing enzyme modifications and
inactivation. Low molecular mass thiols are shown to reduce enzyme inactivation
and NO-induced tyrosine nitration. The present study contributes to the understanding
of the nature of NO reaction with E. coli MnSOD and provides compelling
argument in support of the direct involvement of NO in MnSOD mediated
generation of nitrating species. Interaction of NO with MnSOD may represent a
novel mechanism by which MnSOD protects the cell from deleterious effects
associated with overproduction of NO. However, extensive MnSOD modifications
and inactivation associated with a prolonged exposure to NO will amplify toxic
effects caused by elevated cell superoxide and NO levels.
PB  - IOS Press
T2  - NATO Science Series, Series I: Life and Behavioural Sciences - Free Radicals and Diseases: Gene Expression, Cellular Metabolism and Pathophysiology
T1  - The effects of nitric oxide and peroxynitrite on MnSOD (E. coli)
VL  - 367
SP  - 61
EP  - 69
UR  - https://hdl.handle.net/21.15107/rcub_cer_6509
ER  - 

@inbook{
author = "Filipović, Miloš and Stanić, Dragana and Nikolić, Milan and Stojanović, Srđan and Raičević, Smiljana and Niketić, Vesna",
year = "2005",
abstract = "In vitro studies demonstrated that peroxynitrite inactivates both human
recombinant MnSOD (hrMnSOD) and E. coli MnSOD causing enzyme tyrosine
residue(s) nitration. This led to a suggestion that human MnSOD nitration and
inactivation in vivo, detected in various deseases associated with oxidative stress and
overproduction of nitric monoxide (NO)–conditions that favor peroxynitrite
formation–are also caused by peroxynitrite. In a previous study we demonstrated
that the exposure of E. coli MnSOD to NO under the anaerobic conditions causes
NO conversion (dismutation) into reactive nitrosonium (NO
+
) and nitroxyl
(HNO/NO
–
) species, which produce enzyme modifications and inactivation (Niketic
et al., Free Rad. Biol. Med. 27: 992 (1999)). The present study shows that interaction
of NO with E. coli MnSOD leads to the formation of nitrating species capable
of nitrating and oxidizing enzyme tyrosine residues, as well as that these species
are less invasive than peroxynitrite in producing enzyme modifications and
inactivation. Low molecular mass thiols are shown to reduce enzyme inactivation
and NO-induced tyrosine nitration. The present study contributes to the understanding
of the nature of NO reaction with E. coli MnSOD and provides compelling
argument in support of the direct involvement of NO in MnSOD mediated
generation of nitrating species. Interaction of NO with MnSOD may represent a
novel mechanism by which MnSOD protects the cell from deleterious effects
associated with overproduction of NO. However, extensive MnSOD modifications
and inactivation associated with a prolonged exposure to NO will amplify toxic
effects caused by elevated cell superoxide and NO levels.",
publisher = "IOS Press",
journal = "NATO Science Series, Series I: Life and Behavioural Sciences - Free Radicals and Diseases: Gene Expression, Cellular Metabolism and Pathophysiology",
booktitle = "The effects of nitric oxide and peroxynitrite on MnSOD (E. coli)",
volume = "367",
pages = "61-69",
url = "https://hdl.handle.net/21.15107/rcub_cer_6509"
}

Filipović, M., Stanić, D., Nikolić, M., Stojanović, S., Raičević, S.,& Niketić, V.. (2005). The effects of nitric oxide and peroxynitrite on MnSOD (E. coli). in NATO Science Series, Series I: Life and Behavioural Sciences - Free Radicals and Diseases: Gene Expression, Cellular Metabolism and Pathophysiology
IOS Press., 367, 61-69.
https://hdl.handle.net/21.15107/rcub_cer_6509

Filipović M, Stanić D, Nikolić M, Stojanović S, Raičević S, Niketić V. The effects of nitric oxide and peroxynitrite on MnSOD (E. coli). in NATO Science Series, Series I: Life and Behavioural Sciences - Free Radicals and Diseases: Gene Expression, Cellular Metabolism and Pathophysiology. 2005;367:61-69.
https://hdl.handle.net/21.15107/rcub_cer_6509 .

Filipović, Miloš, Stanić, Dragana, Nikolić, Milan, Stojanović, Srđan, Raičević, Smiljana, Niketić, Vesna, "The effects of nitric oxide and peroxynitrite on MnSOD (E. coli)" in NATO Science Series, Series I: Life and Behavioural Sciences - Free Radicals and Diseases: Gene Expression, Cellular Metabolism and Pathophysiology, 367 (2005):61-69,
https://hdl.handle.net/21.15107/rcub_cer_6509 .