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 .

TY  - CONF
AU  - Niketić, Vesna
AU  - Stojanović, Srđan
AU  - Stanić, Dragana
AU  - Nikolić, Milan
AU  - Raičević, Smiljana
AU  - Spasić, Mihajlo
PY  - 2005
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6512
AB  - Rezultati određivanja nitrita, S-nitrozotiola (RSNO) i hidroksilamina (karakterističnih proizvoda NO+
odnosno NO- vrsta) u rastvorima MnSOD (E. coli) i niskomolekulskih tiola tretiranih azot-monoksidom, pod
striktno anaerobnim uslovima, ubedljivo pokazuju da ovaj enzim katalizuje dismutaciju NO u NO+ i NO- vrste.
Generisane RNOS izazivaju modifikacije (uključujući i nitrovanje ostatka tirozina) molekula enzima, što ima za
posledicu inaktivaciju enzima. Modifikacija i inaktivacija MnSOD nastala kao posledica NO dismutacije mnogo
je manja i sporija u odnosu na one izazvane peroksinitritom.
Polazeći od sličnosti u strukturi MnSOD (E. coli) i humane MnSOD pretpostavljeno je da i humana
MnSOD katalizuje NO dismutaciju, te da ostatak cisteina u blizini aktivnog centra molekula enzima reaguje
primarno sa generisanim RNOS, usporavajući tako nitrovanje ostatka tirozina u aktivnom mestu, a time i
inaktivaciju enzima. Ponašanje MnSOD kao NO dismutaze imalo bi protektivnu ulogu u uslovima prekomerne
produkcije NO, jer bi sprečavalo njegovu transformaciju u štetne RNOS.
PB  - Belgrade : Serbian Chemical Society
C3  - Kratki izvodi radova - 43. Savetovanje Srpskog hemijskog društva, 24. i 25. januar 2005, Beograd
T1  - Da li bi mangan superoksid dismutaza (MnSOD) mogla da ima ulogu NO dismutaze?
T1  - Could manganese superoxide dismutase (MnSOD) play a role as NO dismutase?
SP  - 117
EP  - 120
UR  - https://hdl.handle.net/21.15107/rcub_cer_6512
ER  - 

@conference{
author = "Niketić, Vesna and Stojanović, Srđan and Stanić, Dragana and Nikolić, Milan and Raičević, Smiljana and Spasić, Mihajlo",
year = "2005",
abstract = "Rezultati određivanja nitrita, S-nitrozotiola (RSNO) i hidroksilamina (karakterističnih proizvoda NO+
odnosno NO- vrsta) u rastvorima MnSOD (E. coli) i niskomolekulskih tiola tretiranih azot-monoksidom, pod
striktno anaerobnim uslovima, ubedljivo pokazuju da ovaj enzim katalizuje dismutaciju NO u NO+ i NO- vrste.
Generisane RNOS izazivaju modifikacije (uključujući i nitrovanje ostatka tirozina) molekula enzima, što ima za
posledicu inaktivaciju enzima. Modifikacija i inaktivacija MnSOD nastala kao posledica NO dismutacije mnogo
je manja i sporija u odnosu na one izazvane peroksinitritom.
Polazeći od sličnosti u strukturi MnSOD (E. coli) i humane MnSOD pretpostavljeno je da i humana
MnSOD katalizuje NO dismutaciju, te da ostatak cisteina u blizini aktivnog centra molekula enzima reaguje
primarno sa generisanim RNOS, usporavajući tako nitrovanje ostatka tirozina u aktivnom mestu, a time i
inaktivaciju enzima. Ponašanje MnSOD kao NO dismutaze imalo bi protektivnu ulogu u uslovima prekomerne
produkcije NO, jer bi sprečavalo njegovu transformaciju u štetne RNOS.",
publisher = "Belgrade : Serbian Chemical Society",
journal = "Kratki izvodi radova - 43. Savetovanje Srpskog hemijskog društva, 24. i 25. januar 2005, Beograd",
title = "Da li bi mangan superoksid dismutaza (MnSOD) mogla da ima ulogu NO dismutaze?, Could manganese superoxide dismutase (MnSOD) play a role as NO dismutase?",
pages = "117-120",
url = "https://hdl.handle.net/21.15107/rcub_cer_6512"
}

Niketić, V., Stojanović, S., Stanić, D., Nikolić, M., Raičević, S.,& Spasić, M.. (2005). Da li bi mangan superoksid dismutaza (MnSOD) mogla da ima ulogu NO dismutaze?. in Kratki izvodi radova - 43. Savetovanje Srpskog hemijskog društva, 24. i 25. januar 2005, Beograd
Belgrade : Serbian Chemical Society., 117-120.
https://hdl.handle.net/21.15107/rcub_cer_6512

Niketić V, Stojanović S, Stanić D, Nikolić M, Raičević S, Spasić M. Da li bi mangan superoksid dismutaza (MnSOD) mogla da ima ulogu NO dismutaze?. in Kratki izvodi radova - 43. Savetovanje Srpskog hemijskog društva, 24. i 25. januar 2005, Beograd. 2005;:117-120.
https://hdl.handle.net/21.15107/rcub_cer_6512 .

Niketić, Vesna, Stojanović, Srđan, Stanić, Dragana, Nikolić, Milan, Raičević, Smiljana, Spasić, Mihajlo, "Da li bi mangan superoksid dismutaza (MnSOD) mogla da ima ulogu NO dismutaze?" in Kratki izvodi radova - 43. Savetovanje Srpskog hemijskog društva, 24. i 25. januar 2005, Beograd (2005):117-120,
https://hdl.handle.net/21.15107/rcub_cer_6512 .

TY  - JOUR
AU  - Stojanović, Srđan
AU  - Stanić, Dragana
AU  - Nikolić, Milan
AU  - Raičević, Smiljana
AU  - Spasić, Mihajlo B.
AU  - Niketić, Vesna
PY  - 2005
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/215
AB  - The peroxynitrite-induced nitration of manganese superoxide dismutase (MnSOD) tyrosine residue, which causes enzyme inactivation, is well established. This led to suggestions that MnSOD nitration and inactivation in vivo, detected in various diseases associated with oxidative stress and overproduction of nitric monoxide (NO), conditions which favor peroxynitrite formation, is also caused by peroxynitrite. However, our previous in vitro study demonstrated that exposure of MnSOD to NO led to NO conversion into nitrosonium (NO+) and nitroxyl (NO–) species, which caused enzyme modifications and inactivation. Here it is reported that MnSOD is tyrosine nitrated upon exposure to NO, as well as that MnSOD nitration contributes to inactivation of the enzyme. Collectively, these observations provide a compelling argument supporting the generation of nitrating species in MnSOD exposed to NO and shed a new light on MnSOD tyrosine nitration and inactivation in vivo. This may represent a novel mechanism by which MnSOD protects cell from deleterious effects associated with overproduction of NO. However, extensive MnSOD modification and inactivation associated with prolonged exposure to NO will amplify the toxic effects caused by increased cell superoxide and NO levels.
AB  - Dobro je poznato da peroksinitrit izaziva nitrovanje ostataka tirozina u mangan-superoksid- dismutazi (MnSOD) što dovodi do inaktivacije enzima. Pokazano je da nitrovanje i inaktivacija MnSOD-a nastaje u raznim bolestima za koje je karakteristič an oksidativni stres i povećana produkcija azot-monoksida (NO). Pošto se pri ovim uslovima očekuje nastajanje peroksinitrita predloženo je da peroksinitrit izaziva nitrovanje i inaktivaciju MnSOD in vivo. U našem prethodnom radu pokazali smo da MnSOD katalizuje transformaciju NO u nitrozonijum (NO+) i nitroksil (NO–) reaktivne vrste, te identifikovali neke od modifikacija molekula enzima koje pri tome nastaju izazivajući njegovu inaktivaciju. U ovom radu je pokazano da pri izlaganju MnSOD azot-monoksidu dolazi i do nitrovanja ostatka tirozina u molekulu enzima, što doprinosi njegovoj inaktivaciji. Ovi rezultati ukazuju da pri interakciji MnSOD sa NO dolazi do nastajanja nitrujućih vrsta, što baca novo svetlo na proces nitrovanja ostataka tirozina i inaktivaciju MnSOD in vivo. Ovo može da predstavlja novi mehanizam kojim MnSOD štiti ćeliju odštetnih efekata izazvanih hiperprodukcijom azot-monoksida. Međutim ekstenzivne modifikacije i inaktivacija MnSOD do kojih dolazi pri produženom izlaganju enzima NO, uvećaće toksične efekte izazvane povećanim koncentracijama superoksida i NO u ćeliji.
PB  - Serbian Chemical Society
T2  - Journal of the Serbian Chemical Society
T1  - Manganese superoxide dismutase (MnSOD) catalyzes NO-dependent tyrosine residue nitration
T1  - Mangan-superoksid-dismutaza (MnSOD) katalizuje NO-zavisno nitrovanje ostatka tirozina
VL  - 70
IS  - 4
SP  - 601
EP  - 608
DO  - 10.2298/JSC0504601S
ER  - 

@article{
author = "Stojanović, Srđan and Stanić, Dragana and Nikolić, Milan and Raičević, Smiljana and Spasić, Mihajlo B. and Niketić, Vesna",
year = "2005",
abstract = "The peroxynitrite-induced nitration of manganese superoxide dismutase (MnSOD) tyrosine residue, which causes enzyme inactivation, is well established. This led to suggestions that MnSOD nitration and inactivation in vivo, detected in various diseases associated with oxidative stress and overproduction of nitric monoxide (NO), conditions which favor peroxynitrite formation, is also caused by peroxynitrite. However, our previous in vitro study demonstrated that exposure of MnSOD to NO led to NO conversion into nitrosonium (NO+) and nitroxyl (NO–) species, which caused enzyme modifications and inactivation. Here it is reported that MnSOD is tyrosine nitrated upon exposure to NO, as well as that MnSOD nitration contributes to inactivation of the enzyme. Collectively, these observations provide a compelling argument supporting the generation of nitrating species in MnSOD exposed to NO and shed a new light on MnSOD tyrosine nitration and inactivation in vivo. This may represent a novel mechanism by which MnSOD protects cell from deleterious effects associated with overproduction of NO. However, extensive MnSOD modification and inactivation associated with prolonged exposure to NO will amplify the toxic effects caused by increased cell superoxide and NO levels., Dobro je poznato da peroksinitrit izaziva nitrovanje ostataka tirozina u mangan-superoksid- dismutazi (MnSOD) što dovodi do inaktivacije enzima. Pokazano je da nitrovanje i inaktivacija MnSOD-a nastaje u raznim bolestima za koje je karakteristič an oksidativni stres i povećana produkcija azot-monoksida (NO). Pošto se pri ovim uslovima očekuje nastajanje peroksinitrita predloženo je da peroksinitrit izaziva nitrovanje i inaktivaciju MnSOD in vivo. U našem prethodnom radu pokazali smo da MnSOD katalizuje transformaciju NO u nitrozonijum (NO+) i nitroksil (NO–) reaktivne vrste, te identifikovali neke od modifikacija molekula enzima koje pri tome nastaju izazivajući njegovu inaktivaciju. U ovom radu je pokazano da pri izlaganju MnSOD azot-monoksidu dolazi i do nitrovanja ostatka tirozina u molekulu enzima, što doprinosi njegovoj inaktivaciji. Ovi rezultati ukazuju da pri interakciji MnSOD sa NO dolazi do nastajanja nitrujućih vrsta, što baca novo svetlo na proces nitrovanja ostataka tirozina i inaktivaciju MnSOD in vivo. Ovo može da predstavlja novi mehanizam kojim MnSOD štiti ćeliju odštetnih efekata izazvanih hiperprodukcijom azot-monoksida. Međutim ekstenzivne modifikacije i inaktivacija MnSOD do kojih dolazi pri produženom izlaganju enzima NO, uvećaće toksične efekte izazvane povećanim koncentracijama superoksida i NO u ćeliji.",
publisher = "Serbian Chemical Society",
journal = "Journal of the Serbian Chemical Society",
title = "Manganese superoxide dismutase (MnSOD) catalyzes NO-dependent tyrosine residue nitration, Mangan-superoksid-dismutaza (MnSOD) katalizuje NO-zavisno nitrovanje ostatka tirozina",
volume = "70",
number = "4",
pages = "601-608",
doi = "10.2298/JSC0504601S"
}

Stojanović, S., Stanić, D., Nikolić, M., Raičević, S., Spasić, M. B.,& Niketić, V.. (2005). Manganese superoxide dismutase (MnSOD) catalyzes NO-dependent tyrosine residue nitration. in Journal of the Serbian Chemical Society
Serbian Chemical Society., 70(4), 601-608.
https://doi.org/10.2298/JSC0504601S

Stojanović S, Stanić D, Nikolić M, Raičević S, Spasić MB, Niketić V. Manganese superoxide dismutase (MnSOD) catalyzes NO-dependent tyrosine residue nitration. in Journal of the Serbian Chemical Society. 2005;70(4):601-608.
doi:10.2298/JSC0504601S .

Stojanović, Srđan, Stanić, Dragana, Nikolić, Milan, Raičević, Smiljana, Spasić, Mihajlo B., Niketić, Vesna, "Manganese superoxide dismutase (MnSOD) catalyzes NO-dependent tyrosine residue nitration" in Journal of the Serbian Chemical Society, 70, no. 4 (2005):601-608,
https://doi.org/10.2298/JSC0504601S . .

TY  - CONF
AU  - Stanić, Dragana
AU  - Nikolić, Milan
AU  - Stojanović, Srđan
AU  - Raičević, Smiljana
AU  - Niketić, Vesna
PY  - 2003
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6535
AB  - Our results demonstrate that MnSOD (E. coli)-stimulated generation of NO+ and NO- species is associated with nitration of enzyme tyrosine residues and dityrosinc formation, which cause enzyme inactivation. This represents to our knowledge entirely knew mode of NO-mediated tyrosine nitration. Peroxynitritc treatment of MnSOD (E. coli) caused nitration of tyrosine residues and loss of activity, but not dityrosinc formation. Considering high structural similarities of active centers of these two enzymes, observed differences arc surprising. Wc assume that different reactivity of MnSOD (E. coli) toward NO and ONOO- comparing to that of hMnSOD may be (partly) explained by higher flexibility of its (dimeric) structure comparing to that of hMnSOD, which is tetramer.
PB  - Turkish Biochemical Society
C3  - Turkish Journal of Biochemistry
T1  - The effects of nitric oxide (NO) and peroxynitrite on MnSOD (E.coli)
VL  - 28
IS  - 3
SP  - 116
EP  - 117
UR  - https://hdl.handle.net/21.15107/rcub_cer_6535
ER  - 

@conference{
author = "Stanić, Dragana and Nikolić, Milan and Stojanović, Srđan and Raičević, Smiljana and Niketić, Vesna",
year = "2003",
abstract = "Our results demonstrate that MnSOD (E. coli)-stimulated generation of NO+ and NO- species is associated with nitration of enzyme tyrosine residues and dityrosinc formation, which cause enzyme inactivation. This represents to our knowledge entirely knew mode of NO-mediated tyrosine nitration. Peroxynitritc treatment of MnSOD (E. coli) caused nitration of tyrosine residues and loss of activity, but not dityrosinc formation. Considering high structural similarities of active centers of these two enzymes, observed differences arc surprising. Wc assume that different reactivity of MnSOD (E. coli) toward NO and ONOO- comparing to that of hMnSOD may be (partly) explained by higher flexibility of its (dimeric) structure comparing to that of hMnSOD, which is tetramer.",
publisher = "Turkish Biochemical Society",
journal = "Turkish Journal of Biochemistry",
title = "The effects of nitric oxide (NO) and peroxynitrite on MnSOD (E.coli)",
volume = "28",
number = "3",
pages = "116-117",
url = "https://hdl.handle.net/21.15107/rcub_cer_6535"
}

Stanić, D., Nikolić, M., Stojanović, S., Raičević, S.,& Niketić, V.. (2003). The effects of nitric oxide (NO) and peroxynitrite on MnSOD (E.coli). in Turkish Journal of Biochemistry
Turkish Biochemical Society., 28(3), 116-117.
https://hdl.handle.net/21.15107/rcub_cer_6535

Stanić D, Nikolić M, Stojanović S, Raičević S, Niketić V. The effects of nitric oxide (NO) and peroxynitrite on MnSOD (E.coli). in Turkish Journal of Biochemistry. 2003;28(3):116-117.
https://hdl.handle.net/21.15107/rcub_cer_6535 .

Stanić, Dragana, Nikolić, Milan, Stojanović, Srđan, Raičević, Smiljana, Niketić, Vesna, "The effects of nitric oxide (NO) and peroxynitrite on MnSOD (E.coli)" in Turkish Journal of Biochemistry, 28, no. 3 (2003):116-117,
https://hdl.handle.net/21.15107/rcub_cer_6535 .