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  - 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 .

TY  - CONF
AU  - Stanić, Dragana
AU  - Nikolić, Milan
AU  - Niketić, Vesna
PY  - 2003
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6536
AB  - Our results demonstrate that exposure of erythrocyte membranes to  insulin cause the activation of membrane protease, as well  as that the formation of GPI-Hb parallels its activity. This,  together with recent findings regarding biochemical  pathway of GPI-protein biosynthesis suggest that the  insulin-activated protease is GPI-transpeptidase which is  able to catalyze, albeit slowly, the transpeptidation, i.e., the  replacement of the carboxy-terminal amino acid(s) residues  of Hb ȕ-chains with GPI as an exogenous nucleophile.
PB  - Turkish Biochemical Society
C3  - Turkish Journal of Biochemistry
T1  - Insulin-activated gpi-transamidase in human  erythrocytes
VL  - 28
IS  - 3
SP  - 116
EP  - 116
UR  - https://hdl.handle.net/21.15107/rcub_cer_6536
ER  - 

@conference{
author = "Stanić, Dragana and Nikolić, Milan and Niketić, Vesna",
year = "2003",
abstract = "Our results demonstrate that exposure of erythrocyte membranes to  insulin cause the activation of membrane protease, as well  as that the formation of GPI-Hb parallels its activity. This,  together with recent findings regarding biochemical  pathway of GPI-protein biosynthesis suggest that the  insulin-activated protease is GPI-transpeptidase which is  able to catalyze, albeit slowly, the transpeptidation, i.e., the  replacement of the carboxy-terminal amino acid(s) residues  of Hb ȕ-chains with GPI as an exogenous nucleophile.",
publisher = "Turkish Biochemical Society",
journal = "Turkish Journal of Biochemistry",
title = "Insulin-activated gpi-transamidase in human  erythrocytes",
volume = "28",
number = "3",
pages = "116-116",
url = "https://hdl.handle.net/21.15107/rcub_cer_6536"
}

Stanić, D., Nikolić, M.,& Niketić, V.. (2003). Insulin-activated gpi-transamidase in human  erythrocytes. in Turkish Journal of Biochemistry
Turkish Biochemical Society., 28(3), 116-116.
https://hdl.handle.net/21.15107/rcub_cer_6536

Stanić D, Nikolić M, Niketić V. Insulin-activated gpi-transamidase in human  erythrocytes. in Turkish Journal of Biochemistry. 2003;28(3):116-116.
https://hdl.handle.net/21.15107/rcub_cer_6536 .

Stanić, Dragana, Nikolić, Milan, Niketić, Vesna, "Insulin-activated gpi-transamidase in human  erythrocytes" in Turkish Journal of Biochemistry, 28, no. 3 (2003):116-116,
https://hdl.handle.net/21.15107/rcub_cer_6536 .

TY  - CONF
AU  - Nikolić, Milan
AU  - Stanić, Dragana
AU  - Niketić, Vesna
PY  - 2003
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6537
AB  - Our results demonstrate that in  contrast to Ch and PL contents of RBC membrane which  are confined to a narrow range, the lipid levels estimated in  intact RBCs showed more variation: the lowest individual  values for RBC lipids corresponded to those found in  membrane, whereas in RBCs with higher lipid contents the  “excess” was found in hemolysates
PB  - Turkish Biochemical Society
C3  - Turkish Journal of Biochemistry
T1  - Cholesterol bound to hemoglobin in normal human erythrocytes
VL  - 28
IS  - 3
SP  - 117
EP  - 117
UR  - https://hdl.handle.net/21.15107/rcub_cer_6537
ER  - 

@conference{
author = "Nikolić, Milan and Stanić, Dragana and Niketić, Vesna",
year = "2003",
abstract = "Our results demonstrate that in  contrast to Ch and PL contents of RBC membrane which  are confined to a narrow range, the lipid levels estimated in  intact RBCs showed more variation: the lowest individual  values for RBC lipids corresponded to those found in  membrane, whereas in RBCs with higher lipid contents the  “excess” was found in hemolysates",
publisher = "Turkish Biochemical Society",
journal = "Turkish Journal of Biochemistry",
title = "Cholesterol bound to hemoglobin in normal human erythrocytes",
volume = "28",
number = "3",
pages = "117-117",
url = "https://hdl.handle.net/21.15107/rcub_cer_6537"
}

Nikolić, M., Stanić, D.,& Niketić, V.. (2003). Cholesterol bound to hemoglobin in normal human erythrocytes. in Turkish Journal of Biochemistry
Turkish Biochemical Society., 28(3), 117-117.
https://hdl.handle.net/21.15107/rcub_cer_6537

Nikolić M, Stanić D, Niketić V. Cholesterol bound to hemoglobin in normal human erythrocytes. in Turkish Journal of Biochemistry. 2003;28(3):117-117.
https://hdl.handle.net/21.15107/rcub_cer_6537 .

Nikolić, Milan, Stanić, Dragana, Niketić, Vesna, "Cholesterol bound to hemoglobin in normal human erythrocytes" in Turkish Journal of Biochemistry, 28, no. 3 (2003):117-117,
https://hdl.handle.net/21.15107/rcub_cer_6537 .

TY  - CONF
AU  - Stojanović, Srđan
AU  - Pejin, Boris
AU  - Stanimirović, Bojana
AU  - Niketić, Vesna
PY  - 2001
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6578
AB  - U našim ranijim radovima utvrdili smo da pri izlaganju cerebrospinalne tečnosti (CSF) azot monoksidu in vitro dolazi do njegove dismutacije u NO+ i NO' vrste. CSF sadrži tzv "slobodno" gvoždje u mikromoiarnim koncentracijama kao i visoke koncentracije niza konstitueanata koji predstavljaju potencijalne ligande za slobodno gvoždje. Kako mokraćna kiselina gradi stabilne komplekse sa jonima gvoždja, a kako su i slobodno gvoždje i mokraćna kiselina široko rasprostranjeni u biološkim sistemima, u ovom radu smo ispitivali da li ovi kompleksi pri simuliranim fiziološkim uslovima katalizuju dismutaciju NO, te da li nastale reaktivne vrste mogu da izazovu modifikaciju proteina prisutnih u reakcionoj smeši. Da bismo to postigli ispitivali smo modifikacije globina u rastvoru izloženom NO sa i bez prisustva jona gvoždja (0.8 uM) i mokraćne kiseline (400 uM). Modifikacija globina je praćena primenom elektroforetskih tehnika i odredjivanjem stepena modifikacije SH grupa nastajanjem S-nitrozo derivata.
Dobijeni rezultati su uporedjeni sa rezultatima modifikacije methemoglobina (metHb) izloženog NO. Za metHb je poznato da gradi nitrozo komplekse u kojima koordinovani NO ima NO* karakter. Dobijeni rezultati pokazuju da je stepen modifikacije globina izazvan NO* i NO' vrstama nastalirn dismutacijom NO u sistemu Fe/mokraćna kiselina znatno veći nego kod metHb tretiranog sa NO. G slučaju metHb dolazi samo do reakcije SH grupe u položaju (3-93 molekula Hb, dok u slučaju globina koji je izložen NO u prisustvu Fe/mokraćna kiselina, dolazi pored ove, do modifikacije niza bočnih ostataka aminokiselina. S obzirom da su nivoi gvoždja I mokraćne kiseline povećani u nizu patološldh stanja dobijeni rezultati ukazuju na potencijalni značaj dismutacije NO za razumevanje patološke uloge NO u ovim stanjima.
PB  - Belgrade : Serbian Chemical Society
C3  - XL savetovanje Srpskog hemijskog društva, Izvodi radova 18 i 19 januar 2001, Novi Sad
T1  - Dismutacija NO u NO+ i NO- vrste katalizovana jonima gvožđa u prisustvu mokraćne kiseline
SP  - 16
EP  - 16
UR  - https://hdl.handle.net/21.15107/rcub_cer_6578
ER  - 

@conference{
author = "Stojanović, Srđan and Pejin, Boris and Stanimirović, Bojana and Niketić, Vesna",
year = "2001",
abstract = "U našim ranijim radovima utvrdili smo da pri izlaganju cerebrospinalne tečnosti (CSF) azot monoksidu in vitro dolazi do njegove dismutacije u NO+ i NO' vrste. CSF sadrži tzv "slobodno" gvoždje u mikromoiarnim koncentracijama kao i visoke koncentracije niza konstitueanata koji predstavljaju potencijalne ligande za slobodno gvoždje. Kako mokraćna kiselina gradi stabilne komplekse sa jonima gvoždja, a kako su i slobodno gvoždje i mokraćna kiselina široko rasprostranjeni u biološkim sistemima, u ovom radu smo ispitivali da li ovi kompleksi pri simuliranim fiziološkim uslovima katalizuju dismutaciju NO, te da li nastale reaktivne vrste mogu da izazovu modifikaciju proteina prisutnih u reakcionoj smeši. Da bismo to postigli ispitivali smo modifikacije globina u rastvoru izloženom NO sa i bez prisustva jona gvoždja (0.8 uM) i mokraćne kiseline (400 uM). Modifikacija globina je praćena primenom elektroforetskih tehnika i odredjivanjem stepena modifikacije SH grupa nastajanjem S-nitrozo derivata.
Dobijeni rezultati su uporedjeni sa rezultatima modifikacije methemoglobina (metHb) izloženog NO. Za metHb je poznato da gradi nitrozo komplekse u kojima koordinovani NO ima NO* karakter. Dobijeni rezultati pokazuju da je stepen modifikacije globina izazvan NO* i NO' vrstama nastalirn dismutacijom NO u sistemu Fe/mokraćna kiselina znatno veći nego kod metHb tretiranog sa NO. G slučaju metHb dolazi samo do reakcije SH grupe u položaju (3-93 molekula Hb, dok u slučaju globina koji je izložen NO u prisustvu Fe/mokraćna kiselina, dolazi pored ove, do modifikacije niza bočnih ostataka aminokiselina. S obzirom da su nivoi gvoždja I mokraćne kiseline povećani u nizu patološldh stanja dobijeni rezultati ukazuju na potencijalni značaj dismutacije NO za razumevanje patološke uloge NO u ovim stanjima.",
publisher = "Belgrade : Serbian Chemical Society",
journal = "XL savetovanje Srpskog hemijskog društva, Izvodi radova 18 i 19 januar 2001, Novi Sad",
title = "Dismutacija NO u NO+ i NO- vrste katalizovana jonima gvožđa u prisustvu mokraćne kiseline",
pages = "16-16",
url = "https://hdl.handle.net/21.15107/rcub_cer_6578"
}

Stojanović, S., Pejin, B., Stanimirović, B.,& Niketić, V.. (2001). Dismutacija NO u NO+ i NO- vrste katalizovana jonima gvožđa u prisustvu mokraćne kiseline. in XL savetovanje Srpskog hemijskog društva, Izvodi radova 18 i 19 januar 2001, Novi Sad
Belgrade : Serbian Chemical Society., 16-16.
https://hdl.handle.net/21.15107/rcub_cer_6578

Stojanović S, Pejin B, Stanimirović B, Niketić V. Dismutacija NO u NO+ i NO- vrste katalizovana jonima gvožđa u prisustvu mokraćne kiseline. in XL savetovanje Srpskog hemijskog društva, Izvodi radova 18 i 19 januar 2001, Novi Sad. 2001;:16-16.
https://hdl.handle.net/21.15107/rcub_cer_6578 .

Stojanović, Srđan, Pejin, Boris, Stanimirović, Bojana, Niketić, Vesna, "Dismutacija NO u NO+ i NO- vrste katalizovana jonima gvožđa u prisustvu mokraćne kiseline" in XL savetovanje Srpskog hemijskog društva, Izvodi radova 18 i 19 januar 2001, Novi Sad (2001):16-16,
https://hdl.handle.net/21.15107/rcub_cer_6578 .

TY  - CONF
AU  - Stojanović, Srđan
AU  - Niketić, Vesna
AU  - Spasić, Mihajlo
PY  - 1999
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6579
AB  - Reakcije NO sa prelaznim metalima čine osnovu za dejsvo NO u biološkim sistemima.
Reakcije NO sa proteinima koji sadrže hem intenzivno su izučavane. Medjutim, reakcije NO sa drugim metalnim centrima koji se nalaze u biološkim sistemima mnogo su manje ispitivane. Mi smo nedavno pokazali da pri tetiranju Mn i FeSOD sa NO nastaju reaktivni nitrozil kompleksi koji dismutuju NO dajući NO+ i NO’ jone.1 Pored toga, pronašli smo da se u cerebrospinalnoj tečnosti (CSF) nalaze supstance male molekulske mase koje takodje dismutuju NO. Pošto su nitrozo kompleksi gvoždja i aminokiselina opisani u literaturi, a pošto CSF sadrži visoke koncentracije gvoždja (ca. 0.8 pM) i raznih aminokiselina ( ca. 5 - 440 pM) u ovom radu smo ispitivali da li kompleksi gvoždja i aminokiselina imaju sposobnost da dismutuju NO. Da bismo to postigli, razne aminokiseline (ca 10 pM) i Fe2+ (0.8 pM) u 50 mM fosfatnom puferu pH 7.3 su izlagane NO pod anaerobnim uslovima do 6 sati. Dismutacija NO je utvrdjena na osnovu nastajanja značajnih količina nitrita, sporednog proizvoda reakcije NO+ i NO' sa vodom i NO.
Zaključeno je da nitrozo kompleksi gvoždja i aminokiselina vrše efikasnu dlsmutaclju NO: neki kompleksi su davali i do 50 pmol/pmol Fe2+/min nitrita. Efikasnost ovih kompleksa da dismutuju NO prevazilazi efikasnost FeSOD. Važno je primetiti da je ovo suprotno od ponašanja Cu2 + kompleksa aminokiselina koji dismutuju O2 ' , ali mnogo manje efikasno od Cu/ZnSOD. (Potencijalni) biohemijski značaj opisanih rezultata biće ukratko diskutovan.
PB  - Belgrade : Serbian Chemical Society
C3  - 6. jugoslovenski simpozijum biohemije, Program, Izvodi radova, 15-17 oktobar 1999, Beograd
T1  - Dismutacija azot oksida (NO) kompleksima gvožđa i aminokiselina
SP  - 52
EP  - 52
UR  - https://hdl.handle.net/21.15107/rcub_cer_6579
ER  - 

@conference{
author = "Stojanović, Srđan and Niketić, Vesna and Spasić, Mihajlo",
year = "1999",
abstract = "Reakcije NO sa prelaznim metalima čine osnovu za dejsvo NO u biološkim sistemima.
Reakcije NO sa proteinima koji sadrže hem intenzivno su izučavane. Medjutim, reakcije NO sa drugim metalnim centrima koji se nalaze u biološkim sistemima mnogo su manje ispitivane. Mi smo nedavno pokazali da pri tetiranju Mn i FeSOD sa NO nastaju reaktivni nitrozil kompleksi koji dismutuju NO dajući NO+ i NO’ jone.1 Pored toga, pronašli smo da se u cerebrospinalnoj tečnosti (CSF) nalaze supstance male molekulske mase koje takodje dismutuju NO. Pošto su nitrozo kompleksi gvoždja i aminokiselina opisani u literaturi, a pošto CSF sadrži visoke koncentracije gvoždja (ca. 0.8 pM) i raznih aminokiselina ( ca. 5 - 440 pM) u ovom radu smo ispitivali da li kompleksi gvoždja i aminokiselina imaju sposobnost da dismutuju NO. Da bismo to postigli, razne aminokiseline (ca 10 pM) i Fe2+ (0.8 pM) u 50 mM fosfatnom puferu pH 7.3 su izlagane NO pod anaerobnim uslovima do 6 sati. Dismutacija NO je utvrdjena na osnovu nastajanja značajnih količina nitrita, sporednog proizvoda reakcije NO+ i NO' sa vodom i NO.
Zaključeno je da nitrozo kompleksi gvoždja i aminokiselina vrše efikasnu dlsmutaclju NO: neki kompleksi su davali i do 50 pmol/pmol Fe2+/min nitrita. Efikasnost ovih kompleksa da dismutuju NO prevazilazi efikasnost FeSOD. Važno je primetiti da je ovo suprotno od ponašanja Cu2 + kompleksa aminokiselina koji dismutuju O2 ' , ali mnogo manje efikasno od Cu/ZnSOD. (Potencijalni) biohemijski značaj opisanih rezultata biće ukratko diskutovan.",
publisher = "Belgrade : Serbian Chemical Society",
journal = "6. jugoslovenski simpozijum biohemije, Program, Izvodi radova, 15-17 oktobar 1999, Beograd",
title = "Dismutacija azot oksida (NO) kompleksima gvožđa i aminokiselina",
pages = "52-52",
url = "https://hdl.handle.net/21.15107/rcub_cer_6579"
}

Stojanović, S., Niketić, V.,& Spasić, M.. (1999). Dismutacija azot oksida (NO) kompleksima gvožđa i aminokiselina. in 6. jugoslovenski simpozijum biohemije, Program, Izvodi radova, 15-17 oktobar 1999, Beograd
Belgrade : Serbian Chemical Society., 52-52.
https://hdl.handle.net/21.15107/rcub_cer_6579

Stojanović S, Niketić V, Spasić M. Dismutacija azot oksida (NO) kompleksima gvožđa i aminokiselina. in 6. jugoslovenski simpozijum biohemije, Program, Izvodi radova, 15-17 oktobar 1999, Beograd. 1999;:52-52.
https://hdl.handle.net/21.15107/rcub_cer_6579 .

Stojanović, Srđan, Niketić, Vesna, Spasić, Mihajlo, "Dismutacija azot oksida (NO) kompleksima gvožđa i aminokiselina" in 6. jugoslovenski simpozijum biohemije, Program, Izvodi radova, 15-17 oktobar 1999, Beograd (1999):52-52,
https://hdl.handle.net/21.15107/rcub_cer_6579 .

TY  - CONF
AU  - Niketić, Svetozar
AU  - Niketić, Vesna
AU  - Stojanović, Srđan
AU  - Spasić, Mihajlo
PY  - 1999
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6538
AB  - Ligand field analysis (in the AOM formalism) of Mn(ll, lll) in seven Mn SOD structures reported in the Brookhaven PDB show non-negligible differences in d-orbital energies. The results are equally affected by the azimuthal deformations of the coordination polyhedron, as well as by the orientations of the His imidazole rings with respect to the Mn-N bonds or of the Asp C700 fragment with resepct to the Mn-O bond, since both N and O ligators are behaving as anisotropic pi acceptors and donors, respectively. The orbital energies were used to gauge the ability of manganese to gain or loose an electron in an attempt to predict changes in the redox potential and to correlate these predictions with the data on the kinetics of dismutation recations. The resuls are used to explain our recent observation that E. coli Mn SOD exposed to nitric oxide (NO) in vitro catalyzes its dismutation.
PB  - Association of Greek Chemists
C3  - Book of abstracts - 5th International Symposium on Applied Bioinorganic Chemistry (5ISABC), Corfu, Greece
T1  - Ligand field regulation of manganese redox potential in MnSODs
SP  - 52
EP  - 52
UR  - https://hdl.handle.net/21.15107/rcub_cer_6538
ER  - 

@conference{
author = "Niketić, Svetozar and Niketić, Vesna and Stojanović, Srđan and Spasić, Mihajlo",
year = "1999",
abstract = "Ligand field analysis (in the AOM formalism) of Mn(ll, lll) in seven Mn SOD structures reported in the Brookhaven PDB show non-negligible differences in d-orbital energies. The results are equally affected by the azimuthal deformations of the coordination polyhedron, as well as by the orientations of the His imidazole rings with respect to the Mn-N bonds or of the Asp C700 fragment with resepct to the Mn-O bond, since both N and O ligators are behaving as anisotropic pi acceptors and donors, respectively. The orbital energies were used to gauge the ability of manganese to gain or loose an electron in an attempt to predict changes in the redox potential and to correlate these predictions with the data on the kinetics of dismutation recations. The resuls are used to explain our recent observation that E. coli Mn SOD exposed to nitric oxide (NO) in vitro catalyzes its dismutation.",
publisher = "Association of Greek Chemists",
journal = "Book of abstracts - 5th International Symposium on Applied Bioinorganic Chemistry (5ISABC), Corfu, Greece",
title = "Ligand field regulation of manganese redox potential in MnSODs",
pages = "52-52",
url = "https://hdl.handle.net/21.15107/rcub_cer_6538"
}

Niketić, S., Niketić, V., Stojanović, S.,& Spasić, M.. (1999). Ligand field regulation of manganese redox potential in MnSODs. in Book of abstracts - 5th International Symposium on Applied Bioinorganic Chemistry (5ISABC), Corfu, Greece
Association of Greek Chemists., 52-52.
https://hdl.handle.net/21.15107/rcub_cer_6538

Niketić S, Niketić V, Stojanović S, Spasić M. Ligand field regulation of manganese redox potential in MnSODs. in Book of abstracts - 5th International Symposium on Applied Bioinorganic Chemistry (5ISABC), Corfu, Greece. 1999;:52-52.
https://hdl.handle.net/21.15107/rcub_cer_6538 .

Niketić, Svetozar, Niketić, Vesna, Stojanović, Srđan, Spasić, Mihajlo, "Ligand field regulation of manganese redox potential in MnSODs" in Book of abstracts - 5th International Symposium on Applied Bioinorganic Chemistry (5ISABC), Corfu, Greece (1999):52-52,
https://hdl.handle.net/21.15107/rcub_cer_6538 .

TY  - JOUR
AU  - Niketić, Vesna
AU  - Stojanović, Srđan
AU  - Nikolić, Aleksandra
AU  - Spasić, Mihajlo
AU  - Michelson, A.M.
PY  - 1999
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6508
AB  - The effect of NO treatment in vitro on structural and functional alterations of Cu/Zn, Mn, and Fe type of
SODs was studied. Significant difference in response to NO of Cu/ZnSOD compared to the Mn and Fe types was
demonstrated. Cu/ZnSOD was shown to be stable with respect to NO: even on prolonged exposure, NO produced
negligible effect on its structure and activity. In contrast, both Mn and Fe types were found to be NO-sensitive: exposure
to NO led to their fast and extensive inactivation, which was accompanied by extensive structural alterations, including
(in some of the samples tested) the cleavage of enzyme polypeptide chains, presumably at His residues of the enzyme
metal binding sites. The generation of nitrosonium (NO1) and nitroxyl (NO2) ions in NO treated Mn and FeSODs,
which produce enzyme modifications and inactivation, was demonstrated. The physiological and biomedical significance
of described findings is briefly discussed.
PB  - Elsevier
T2  - Free Radical Biology and Medicine
T1  - Exposure of Mn and FeSODs, but not Cu/ZnSOD, to NO leads to nitrosonium and nitroxyl ions generation which cause enzyme modification and inactivation: an in vitro study
VL  - 27
IS  - 9-10
SP  - 992
EP  - 996
DO  - 10.1016/S0891-5849(98)00256-1
ER  - 

@article{
author = "Niketić, Vesna and Stojanović, Srđan and Nikolić, Aleksandra and Spasić, Mihajlo and Michelson, A.M.",
year = "1999",
abstract = "The effect of NO treatment in vitro on structural and functional alterations of Cu/Zn, Mn, and Fe type of
SODs was studied. Significant difference in response to NO of Cu/ZnSOD compared to the Mn and Fe types was
demonstrated. Cu/ZnSOD was shown to be stable with respect to NO: even on prolonged exposure, NO produced
negligible effect on its structure and activity. In contrast, both Mn and Fe types were found to be NO-sensitive: exposure
to NO led to their fast and extensive inactivation, which was accompanied by extensive structural alterations, including
(in some of the samples tested) the cleavage of enzyme polypeptide chains, presumably at His residues of the enzyme
metal binding sites. The generation of nitrosonium (NO1) and nitroxyl (NO2) ions in NO treated Mn and FeSODs,
which produce enzyme modifications and inactivation, was demonstrated. The physiological and biomedical significance
of described findings is briefly discussed.",
publisher = "Elsevier",
journal = "Free Radical Biology and Medicine",
title = "Exposure of Mn and FeSODs, but not Cu/ZnSOD, to NO leads to nitrosonium and nitroxyl ions generation which cause enzyme modification and inactivation: an in vitro study",
volume = "27",
number = "9-10",
pages = "992-996",
doi = "10.1016/S0891-5849(98)00256-1"
}

Niketić, V., Stojanović, S., Nikolić, A., Spasić, M.,& Michelson, A.M.. (1999). Exposure of Mn and FeSODs, but not Cu/ZnSOD, to NO leads to nitrosonium and nitroxyl ions generation which cause enzyme modification and inactivation: an in vitro study. in Free Radical Biology and Medicine
Elsevier., 27(9-10), 992-996.
https://doi.org/10.1016/S0891-5849(98)00256-1

Niketić V, Stojanović S, Nikolić A, Spasić M, Michelson A. Exposure of Mn and FeSODs, but not Cu/ZnSOD, to NO leads to nitrosonium and nitroxyl ions generation which cause enzyme modification and inactivation: an in vitro study. in Free Radical Biology and Medicine. 1999;27(9-10):992-996.
doi:10.1016/S0891-5849(98)00256-1 .

Niketić, Vesna, Stojanović, Srđan, Nikolić, Aleksandra, Spasić, Mihajlo, Michelson, A.M., "Exposure of Mn and FeSODs, but not Cu/ZnSOD, to NO leads to nitrosonium and nitroxyl ions generation which cause enzyme modification and inactivation: an in vitro study" in Free Radical Biology and Medicine, 27, no. 9-10 (1999):992-996,
https://doi.org/10.1016/S0891-5849(98)00256-1 . .

TY  - CONF
AU  - Marinković, Zorica
AU  - Nikolić, Aleksandra
AU  - Stojanović, Srđan
AU  - Blagojević, Duško
AU  - Niketić, Vesna
AU  - Radunović, A,
AU  - Apostolski, S.
AU  - Spasić, Mihajlo
PY  - 1997
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6540
AB  - The aim of this study was to investigate the content of -SU groups and SOD activity m cerebrospinal fluid (CSF) both in ALS patients and control group, as well as to perform an in vitro lest for CSF NO binding capacity, in same examines. Nitric oxide for in vitro testing was provided by adding 40% sodium nitrite solution in the solution of 10% ferrous sulfate in 50% sulfuric acid. Our results showed significant increase -SH content in CSF of ALS patients in comparison with control group (114 ± 29 nmol -SH/mg proteins in CSF of ALS patients compared with 37 ± 12 nmol - SI Lmg proteins in CSF of controls)(p<0.05). After in vitro saturation of CSF with NO, we noted (he significant decrease of -SH content which was not found in control group. We also found that SOD activity in CSF of ALS patients was higher than in control group (16.1 ±2.8 U7 mg CSF proteins of ALS patients compared to 10.2 ± 2 U/ mg CSF proteins of control group). These results may confirm an increased ROS production in ALS patients without increased NO production.
C3  - 8th International Symposium on ALS/MND, Glasgow
T1  - Content of NO reactive -SH and Superoxide dismutase activity in CSF of ALS patients
UR  - https://hdl.handle.net/21.15107/rcub_cer_6540
ER  - 

@conference{
author = "Marinković, Zorica and Nikolić, Aleksandra and Stojanović, Srđan and Blagojević, Duško and Niketić, Vesna and Radunović, A, and Apostolski, S. and Spasić, Mihajlo",
year = "1997",
abstract = "The aim of this study was to investigate the content of -SU groups and SOD activity m cerebrospinal fluid (CSF) both in ALS patients and control group, as well as to perform an in vitro lest for CSF NO binding capacity, in same examines. Nitric oxide for in vitro testing was provided by adding 40% sodium nitrite solution in the solution of 10% ferrous sulfate in 50% sulfuric acid. Our results showed significant increase -SH content in CSF of ALS patients in comparison with control group (114 ± 29 nmol -SH/mg proteins in CSF of ALS patients compared with 37 ± 12 nmol - SI Lmg proteins in CSF of controls)(p<0.05). After in vitro saturation of CSF with NO, we noted (he significant decrease of -SH content which was not found in control group. We also found that SOD activity in CSF of ALS patients was higher than in control group (16.1 ±2.8 U7 mg CSF proteins of ALS patients compared to 10.2 ± 2 U/ mg CSF proteins of control group). These results may confirm an increased ROS production in ALS patients without increased NO production.",
journal = "8th International Symposium on ALS/MND, Glasgow",
title = "Content of NO reactive -SH and Superoxide dismutase activity in CSF of ALS patients",
url = "https://hdl.handle.net/21.15107/rcub_cer_6540"
}

Marinković, Z., Nikolić, A., Stojanović, S., Blagojević, D., Niketić, V., Radunović, A., Apostolski, S.,& Spasić, M.. (1997). Content of NO reactive -SH and Superoxide dismutase activity in CSF of ALS patients. in 8th International Symposium on ALS/MND, Glasgow.
https://hdl.handle.net/21.15107/rcub_cer_6540

Marinković Z, Nikolić A, Stojanović S, Blagojević D, Niketić V, Radunović A, Apostolski S, Spasić M. Content of NO reactive -SH and Superoxide dismutase activity in CSF of ALS patients. in 8th International Symposium on ALS/MND, Glasgow. 1997;.
https://hdl.handle.net/21.15107/rcub_cer_6540 .

Marinković, Zorica, Nikolić, Aleksandra, Stojanović, Srđan, Blagojević, Duško, Niketić, Vesna, Radunović, A,, Apostolski, S., Spasić, Mihajlo, "Content of NO reactive -SH and Superoxide dismutase activity in CSF of ALS patients" in 8th International Symposium on ALS/MND, Glasgow (1997),
https://hdl.handle.net/21.15107/rcub_cer_6540 .