TY  - JOUR
AU  - Berberina, Luka
AU  - Nikolić, Milan
AU  - Stojanović, Srđan Đ.
AU  - Zlatović, Mario
PY  - 2023
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6269
AB  - The influences of π-π interactions in phycocyanin proteins and their environmental preferences were analyzed. The observations indicate that the majority of the aromatic residues in phycocyanin proteins are involved in π-π interactions. Phenylalanine (Phe) and tyrosine (Tyr) residues were found to be involved in π–π interactions much more frequently than tryptophan (Trp) or histidine (His). Similarly, the Phe-Phe and Tyr-Tyr π–π interacting paiThe influences of π-π interactions in phycocyanin proteins and their environmental preferences were analyzed. The observations indicate that the majority of the aromatic residues in phycocyanin proteins are involved in π-π interactions. Phenylalanine (Phe) and tyrosine (Tyr) residues were found to be involved in π–π interactions much more frequently than tryptophan (Trp) or histidine (His). Similarly, the Phe-Phe and Tyr-Tyr π–π interacting pair had the highest frequency of occurrence. In addition to π-π interactions, the arom­atic residues also form π-networks in phycocyanins. The π–π interactions are most favourable at the pair distance range of 5.5–7 Å, with a clear preference for T-shaped ring arrangements. Using ab initio calculations, we observed that most of the π-π interactions possess energy from 0 to -10 kJ mol-1. Stabil­iz­ation centres for these proteins showed that all residues found in π-π inter­actions are important in locating one or more such centres. π-π interacting resi­dues are evolutionary conserved. The results obtained from this study will be beneficial in further understanding the structural stability and eventual develop­ment of protein engineering of phycocyanins.r had the highest frequency of occurrence. In addition to π-π interactions, the arom­atic residues also form π-networks in phycocyanins. The π–π interactions are most favourable at the pair distance range of 5.5–7 Å, with a clear preference for T-shaped ring arrangements. Using ab initio calculations, we observed that most of the π-π interactions possess energy from 0 to -10 kJ mol-1. Stabil­iz­ation centres for these proteins showed that all residues found in π-π inter­actions are important in locating one or more such centres. π-π interacting resi­dues are evolutionary conserved. The results obtained from this study will be beneficial in further understanding the structural stability and eventual develop­ment of protein engineering of phycocyanins.
PB  - Serbian Chemical Society
T2  - Journal of the Serbian Chemical Society
T1  - On the importance of π–π interactions in structural stability of phycocyanins: Scientific paper
VL  - 88
IS  - 5
SP  - 481
EP  - 494
DO  - 10.2298/JSC221201008B
ER  - 

@article{
author = "Berberina, Luka and Nikolić, Milan and Stojanović, Srđan Đ. and Zlatović, Mario",
year = "2023",
abstract = "The influences of π-π interactions in phycocyanin proteins and their environmental preferences were analyzed. The observations indicate that the majority of the aromatic residues in phycocyanin proteins are involved in π-π interactions. Phenylalanine (Phe) and tyrosine (Tyr) residues were found to be involved in π–π interactions much more frequently than tryptophan (Trp) or histidine (His). Similarly, the Phe-Phe and Tyr-Tyr π–π interacting paiThe influences of π-π interactions in phycocyanin proteins and their environmental preferences were analyzed. The observations indicate that the majority of the aromatic residues in phycocyanin proteins are involved in π-π interactions. Phenylalanine (Phe) and tyrosine (Tyr) residues were found to be involved in π–π interactions much more frequently than tryptophan (Trp) or histidine (His). Similarly, the Phe-Phe and Tyr-Tyr π–π interacting pair had the highest frequency of occurrence. In addition to π-π interactions, the arom­atic residues also form π-networks in phycocyanins. The π–π interactions are most favourable at the pair distance range of 5.5–7 Å, with a clear preference for T-shaped ring arrangements. Using ab initio calculations, we observed that most of the π-π interactions possess energy from 0 to -10 kJ mol-1. Stabil­iz­ation centres for these proteins showed that all residues found in π-π inter­actions are important in locating one or more such centres. π-π interacting resi­dues are evolutionary conserved. The results obtained from this study will be beneficial in further understanding the structural stability and eventual develop­ment of protein engineering of phycocyanins.r had the highest frequency of occurrence. In addition to π-π interactions, the arom­atic residues also form π-networks in phycocyanins. The π–π interactions are most favourable at the pair distance range of 5.5–7 Å, with a clear preference for T-shaped ring arrangements. Using ab initio calculations, we observed that most of the π-π interactions possess energy from 0 to -10 kJ mol-1. Stabil­iz­ation centres for these proteins showed that all residues found in π-π inter­actions are important in locating one or more such centres. π-π interacting resi­dues are evolutionary conserved. The results obtained from this study will be beneficial in further understanding the structural stability and eventual develop­ment of protein engineering of phycocyanins.",
publisher = "Serbian Chemical Society",
journal = "Journal of the Serbian Chemical Society",
title = "On the importance of π–π interactions in structural stability of phycocyanins: Scientific paper",
volume = "88",
number = "5",
pages = "481-494",
doi = "10.2298/JSC221201008B"
}

Berberina, L., Nikolić, M., Stojanović, S. Đ.,& Zlatović, M.. (2023). On the importance of π–π interactions in structural stability of phycocyanins: Scientific paper. in Journal of the Serbian Chemical Society
Serbian Chemical Society., 88(5), 481-494.
https://doi.org/10.2298/JSC221201008B

Berberina L, Nikolić M, Stojanović SĐ, Zlatović M. On the importance of π–π interactions in structural stability of phycocyanins: Scientific paper. in Journal of the Serbian Chemical Society. 2023;88(5):481-494.
doi:10.2298/JSC221201008B .

Berberina, Luka, Nikolić, Milan, Stojanović, Srđan Đ., Zlatović, Mario, "On the importance of π–π interactions in structural stability of phycocyanins: Scientific paper" in Journal of the Serbian Chemical Society, 88, no. 5 (2023):481-494,
https://doi.org/10.2298/JSC221201008B . .

TY  - JOUR
AU  - Stojanović, Srđan Đ.
AU  - Zlatović, Mario
PY  - 2023
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5873
AB  - In the present work, the influences of π–π interactions in superoxide
dismutase (SOD) active centers were analyzed. The majority of the aromatic
residues are involved in π–π interactions. Predominant type of interacting pairs is
His–His and His–Trp pairs. In addition to π–π interactions, π residues also form πnetworks in SOD proteins. The π–π interactions are most favorable at the pair
distance range of 5–7 Å. We observed that most of the π–π interactions shows
stabilization energies in the range −4.2 to −12.6 kJ mol-1
, while the metal assisted
π–π interactions showed an energy in the range −83.7 to −334.7 kJ mol-1
. Most of
the π–π interacting residues were evolutionary conserved and thus probably
important in maintaining the structural stability of proteins through these
interactions. A high percentage of these residues could be considered as
stabilization centers, contributing to the net stability of SOD proteins.
PB  - Belgrade : Serbian Chemical Society
T2  - Journal of the Serbian Chemical Society
T1  - π-π interactions in structural stability: Role in superoxide dismutases
VL  - 88
IS  - 3
SP  - 223
EP  - 235
DO  - 10.2298/JSC220404052S
ER  - 

@article{
author = "Stojanović, Srđan Đ. and Zlatović, Mario",
year = "2023",
abstract = "In the present work, the influences of π–π interactions in superoxide
dismutase (SOD) active centers were analyzed. The majority of the aromatic
residues are involved in π–π interactions. Predominant type of interacting pairs is
His–His and His–Trp pairs. In addition to π–π interactions, π residues also form πnetworks in SOD proteins. The π–π interactions are most favorable at the pair
distance range of 5–7 Å. We observed that most of the π–π interactions shows
stabilization energies in the range −4.2 to −12.6 kJ mol-1
, while the metal assisted
π–π interactions showed an energy in the range −83.7 to −334.7 kJ mol-1
. Most of
the π–π interacting residues were evolutionary conserved and thus probably
important in maintaining the structural stability of proteins through these
interactions. A high percentage of these residues could be considered as
stabilization centers, contributing to the net stability of SOD proteins.",
publisher = "Belgrade : Serbian Chemical Society",
journal = "Journal of the Serbian Chemical Society",
title = "π-π interactions in structural stability: Role in superoxide dismutases",
volume = "88",
number = "3",
pages = "223-235",
doi = "10.2298/JSC220404052S"
}

Stojanović, S. Đ.,& Zlatović, M.. (2023). π-π interactions in structural stability: Role in superoxide dismutases. in Journal of the Serbian Chemical Society
Belgrade : Serbian Chemical Society., 88(3), 223-235.
https://doi.org/10.2298/JSC220404052S

Stojanović SĐ, Zlatović M. π-π interactions in structural stability: Role in superoxide dismutases. in Journal of the Serbian Chemical Society. 2023;88(3):223-235.
doi:10.2298/JSC220404052S .

Stojanović, Srđan Đ., Zlatović, Mario, "π-π interactions in structural stability: Role in superoxide dismutases" in Journal of the Serbian Chemical Society, 88, no. 3 (2023):223-235,
https://doi.org/10.2298/JSC220404052S . .

TY  - JOUR
AU  - Stojanović, Srđan Đ.
AU  - Zlatović, Mario
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5507
AB  - In this study, we have analysed the influence of cation–π interactions on stability and properties of superoxide dismutase (SOD) active centres. The number of interactions formed by arginine is higher than by lysine in the cat­ionic group, while those formed by histidine are comparatively higher in the π group. The energy contribution resulting from most frequent cation–π interact­ions was in the lower range of strong hydrogen bonds. The cation–π interact­ions involving transition metal ions as cation have energy more negative than –418.4 kJ mol-1. The stabilization centres for these proteins showed that all the residues involved in cation–π interactions were important in locating one or more of such centres. The majority of the residues involved in cation–p inter­actions were evolutionarily conserved and might have a significant contribution towards the stability of SOD proteins. The results presented in this work can be very useful for understanding the contribution of cation–π interactions to the stability of SOD active centres.
PB  - Serbian Chemical Society
T2  - The Journal of the Serbian Chemical Society
T1  - Investigations on the role of cation–pi interactions in active centres of superoxide dismutase
VL  - 87
IS  - 4
SP  - 465
EP  - 477
DO  - 10.2298/JSC220109013S
ER  - 

@article{
author = "Stojanović, Srđan Đ. and Zlatović, Mario",
year = "2022",
abstract = "In this study, we have analysed the influence of cation–π interactions on stability and properties of superoxide dismutase (SOD) active centres. The number of interactions formed by arginine is higher than by lysine in the cat­ionic group, while those formed by histidine are comparatively higher in the π group. The energy contribution resulting from most frequent cation–π interact­ions was in the lower range of strong hydrogen bonds. The cation–π interact­ions involving transition metal ions as cation have energy more negative than –418.4 kJ mol-1. The stabilization centres for these proteins showed that all the residues involved in cation–π interactions were important in locating one or more of such centres. The majority of the residues involved in cation–p inter­actions were evolutionarily conserved and might have a significant contribution towards the stability of SOD proteins. The results presented in this work can be very useful for understanding the contribution of cation–π interactions to the stability of SOD active centres.",
publisher = "Serbian Chemical Society",
journal = "The Journal of the Serbian Chemical Society",
title = "Investigations on the role of cation–pi interactions in active centres of superoxide dismutase",
volume = "87",
number = "4",
pages = "465-477",
doi = "10.2298/JSC220109013S"
}

Stojanović, S. Đ.,& Zlatović, M.. (2022). Investigations on the role of cation–pi interactions in active centres of superoxide dismutase. in The Journal of the Serbian Chemical Society
Serbian Chemical Society., 87(4), 465-477.
https://doi.org/10.2298/JSC220109013S

Stojanović SĐ, Zlatović M. Investigations on the role of cation–pi interactions in active centres of superoxide dismutase. in The Journal of the Serbian Chemical Society. 2022;87(4):465-477.
doi:10.2298/JSC220109013S .

Stojanović, Srđan Đ., Zlatović, Mario, "Investigations on the role of cation–pi interactions in active centres of superoxide dismutase" in The Journal of the Serbian Chemical Society, 87, no. 4 (2022):465-477,
https://doi.org/10.2298/JSC220109013S . .

TY  - JOUR
AU  - Berberina, Luka
AU  - Nikolić, Milan
AU  - Stojanović, Srđan Đ.
AU  - Zlatović, Mario
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5864
AB  - The influences of cation-π interactions in phycocyanin proteins and their environmental preferences were analyzed. The number of interactions formed by arginine showed to be higher than those formed by the lysine in the cationic group, while histidine is comparatively higher than phenylalanine and N-terminal residue in the π group. Arg-Tyr and Arg-Phe interacting pairs are predominant among the various pairs analyzed. Cation-π interactions are distance-dependent and can be realized above a wider area above the π ring. We analyzed the energy contribution resulting from cation-π interactions using ab initio calculations. The energy contribution
resulting from the most frequent cation-π interactions was in the lower range of strong hydrogen bonds. The results showed that, while most of their interaction energies lay ranged from -2 to -8 kcal/mol, those energies could be up to -12 - 12 kcal/mol. Stabilization centers for these proteins showed that all residues found in cation-π interactions are important in locating one or more of such centers. In the cation–π interacting residues, 54% of the amino acid residues involved in these interactions might be conserved in phycocyanins. From this study, we infer that cation-π forming residues play an important role in the stability of the multiply commercially used phycocyanin proteins and could help structural biologists and medicinal chemists to design better and safer drugs.
PB  - Elsevier
T2  - Computational Biology and Chemistry
T1  - Influence of cation−π interactions to the structural stability of phycocyanin proteins: A computational study.
VL  - 100
SP  - 107752
DO  - 10.1016/j.compbiolchem.2022.107752
ER  - 

@article{
author = "Berberina, Luka and Nikolić, Milan and Stojanović, Srđan Đ. and Zlatović, Mario",
year = "2022",
abstract = "The influences of cation-π interactions in phycocyanin proteins and their environmental preferences were analyzed. The number of interactions formed by arginine showed to be higher than those formed by the lysine in the cationic group, while histidine is comparatively higher than phenylalanine and N-terminal residue in the π group. Arg-Tyr and Arg-Phe interacting pairs are predominant among the various pairs analyzed. Cation-π interactions are distance-dependent and can be realized above a wider area above the π ring. We analyzed the energy contribution resulting from cation-π interactions using ab initio calculations. The energy contribution
resulting from the most frequent cation-π interactions was in the lower range of strong hydrogen bonds. The results showed that, while most of their interaction energies lay ranged from -2 to -8 kcal/mol, those energies could be up to -12 - 12 kcal/mol. Stabilization centers for these proteins showed that all residues found in cation-π interactions are important in locating one or more of such centers. In the cation–π interacting residues, 54% of the amino acid residues involved in these interactions might be conserved in phycocyanins. From this study, we infer that cation-π forming residues play an important role in the stability of the multiply commercially used phycocyanin proteins and could help structural biologists and medicinal chemists to design better and safer drugs.",
publisher = "Elsevier",
journal = "Computational Biology and Chemistry",
title = "Influence of cation−π interactions to the structural stability of phycocyanin proteins: A computational study.",
volume = "100",
pages = "107752",
doi = "10.1016/j.compbiolchem.2022.107752"
}

Berberina, L., Nikolić, M., Stojanović, S. Đ.,& Zlatović, M.. (2022). Influence of cation−π interactions to the structural stability of phycocyanin proteins: A computational study.. in Computational Biology and Chemistry
Elsevier., 100, 107752.
https://doi.org/10.1016/j.compbiolchem.2022.107752

Berberina L, Nikolić M, Stojanović SĐ, Zlatović M. Influence of cation−π interactions to the structural stability of phycocyanin proteins: A computational study.. in Computational Biology and Chemistry. 2022;100:107752.
doi:10.1016/j.compbiolchem.2022.107752 .

Berberina, Luka, Nikolić, Milan, Stojanović, Srđan Đ., Zlatović, Mario, "Influence of cation−π interactions to the structural stability of phycocyanin proteins: A computational study." in Computational Biology and Chemistry, 100 (2022):107752,
https://doi.org/10.1016/j.compbiolchem.2022.107752 . .

TY  - JOUR
AU  - Stojanović, Srđan Đ.
AU  - Stanić, Dragana
AU  - Nikolić, Milan
AU  - Raicevic, S
AU  - Spasić, Mihajlo B.
AU  - Niketic, V
PY  - 2005
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/713
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 ill 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 ill 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 Soc, Belgrade
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 Đ. and Stanić, Dragana and Nikolić, Milan and Raicevic, S and Spasić, Mihajlo B. and Niketic, V",
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 ill 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 ill 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 Soc, Belgrade",
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. Đ., Stanić, D., Nikolić, M., Raicevic, S., Spasić, M. B.,& Niketic, V.. (2005). Manganese superoxide dismutase (MnSOD) catalyzes NO-dependent tyrosine residue nitration. in Journal of the Serbian Chemical Society
Serbian Chemical Soc, Belgrade., 70(4), 601-608.
https://doi.org/10.2298/JSC0504601S

Stojanović SĐ, Stanić D, Nikolić M, Raicevic S, Spasić MB, Niketic 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 Đ., Stanić, Dragana, Nikolić, Milan, Raicevic, S, Spasić, Mihajlo B., Niketic, V, "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  - JOUR
AU  - Stojanović, Srđan Đ.
AU  - Stanić, Dragana
AU  - Nikolić, Milan
AU  - Spasić, Mihajlo B.
AU  - Niketic, V
PY  - 2004
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/675
AB  - The conversion of NO into its congeners, nitrosonium (NO+) and nitroxyl (HNO/NO-) species, has important consequences in NO metabolism. Dinitrosyl iron complex (DNIC) combined with thiol ligands was shown to catalyze the conversion of NO into NO+, resulting in the synthesis of S-nitrosothiols (RSNO) both in vitro and in vivo. The formation mechanism of DNIC was proposed to involve the intermediate release of nitroxyl. Since the detection of hydroxylamine (as the product of a rapid reaction of HNO/NO- with thiols) is taken as the evidence for nitroxyl generation, we examined the formation of hydroxylamine, RSNO, and nitrite (the product of a rapid reaction of NO+ with water) in neutral solutions containing iron ions and thiols exposed to NO under anaerobic conditions. Hydroxylamine was detected in NO treated solutions of iron ions in the presence of cysteine, but not glutathione (GSH). The addition of urate, a major "free" iron-binding agent in humans, to solutions of GSH and iron ions, and the subsequent treatment of these solutions with NO increased the synthesis of GSNO and resulted in the formation of hydroxylamine. This caused a loss of urate and yielded a novel nitrosative/nitration product. GSH attenuated the urate decomposition to such a degree that it could be reflected as the function of GSH:urate. Results described here contribute to the understanding of the role of iron ions in catalyzing the conversion of NO into HNO/NO- and point to the role of uric acid not previously described. (C) 2004 Elsevier Inc. All rights reserved.
PB  - Academic Press Inc Elsevier Science, San Diego
T2  - Nitric Oxide: Biology and Chemistry
T1  - Iron catalyzed conversion of NO into nitrosonium (NO+) and nitroxyl (HNO/NO-) species
VL  - 11
IS  - 3
SP  - 256
EP  - 262
DO  - 10.1016/j.niox.2004.09.007
ER  - 

@article{
author = "Stojanović, Srđan Đ. and Stanić, Dragana and Nikolić, Milan and Spasić, Mihajlo B. and Niketic, V",
year = "2004",
abstract = "The conversion of NO into its congeners, nitrosonium (NO+) and nitroxyl (HNO/NO-) species, has important consequences in NO metabolism. Dinitrosyl iron complex (DNIC) combined with thiol ligands was shown to catalyze the conversion of NO into NO+, resulting in the synthesis of S-nitrosothiols (RSNO) both in vitro and in vivo. The formation mechanism of DNIC was proposed to involve the intermediate release of nitroxyl. Since the detection of hydroxylamine (as the product of a rapid reaction of HNO/NO- with thiols) is taken as the evidence for nitroxyl generation, we examined the formation of hydroxylamine, RSNO, and nitrite (the product of a rapid reaction of NO+ with water) in neutral solutions containing iron ions and thiols exposed to NO under anaerobic conditions. Hydroxylamine was detected in NO treated solutions of iron ions in the presence of cysteine, but not glutathione (GSH). The addition of urate, a major "free" iron-binding agent in humans, to solutions of GSH and iron ions, and the subsequent treatment of these solutions with NO increased the synthesis of GSNO and resulted in the formation of hydroxylamine. This caused a loss of urate and yielded a novel nitrosative/nitration product. GSH attenuated the urate decomposition to such a degree that it could be reflected as the function of GSH:urate. Results described here contribute to the understanding of the role of iron ions in catalyzing the conversion of NO into HNO/NO- and point to the role of uric acid not previously described. (C) 2004 Elsevier Inc. All rights reserved.",
publisher = "Academic Press Inc Elsevier Science, San Diego",
journal = "Nitric Oxide: Biology and Chemistry",
title = "Iron catalyzed conversion of NO into nitrosonium (NO+) and nitroxyl (HNO/NO-) species",
volume = "11",
number = "3",
pages = "256-262",
doi = "10.1016/j.niox.2004.09.007"
}

Stojanović, S. Đ., Stanić, D., Nikolić, M., Spasić, M. B.,& Niketic, V.. (2004). Iron catalyzed conversion of NO into nitrosonium (NO+) and nitroxyl (HNO/NO-) species. in Nitric Oxide: Biology and Chemistry
Academic Press Inc Elsevier Science, San Diego., 11(3), 256-262.
https://doi.org/10.1016/j.niox.2004.09.007

Stojanović SĐ, Stanić D, Nikolić M, Spasić MB, Niketic V. Iron catalyzed conversion of NO into nitrosonium (NO+) and nitroxyl (HNO/NO-) species. in Nitric Oxide: Biology and Chemistry. 2004;11(3):256-262.
doi:10.1016/j.niox.2004.09.007 .

Stojanović, Srđan Đ., Stanić, Dragana, Nikolić, Milan, Spasić, Mihajlo B., Niketic, V, "Iron catalyzed conversion of NO into nitrosonium (NO+) and nitroxyl (HNO/NO-) species" in Nitric Oxide: Biology and Chemistry, 11, no. 3 (2004):256-262,
https://doi.org/10.1016/j.niox.2004.09.007 . .

TY  - JOUR
AU  - Mandić, Ljuba M.
AU  - Stojanović, Srđan Đ.
AU  - Colovic, A
AU  - Milin, N
PY  - 2000
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/445
AB  - The estimation of glycosylated proteins is useful in the detection and control of long-standing hyperglycemic conditions. In this paper the content of protein-bound glucose was determined in diabetics by spectrophotometric method with phenol-sulphuric acid (PS) and with thiobarbituric acid (TBA). The amounts of protein-bound glucose obtained with the PS reagent (80.6 +/- 22.8 mmol glucose/g protein) were always considerably higher than those obtained by TEA method (3.71 +/- 1.34 mu mol glucose/g protein). The analysis was made of parameters that might have led to such significant difference. It was shown that in the reaction with PS reagent there was an additional dehydration of carbohydrate released during the hydrolysis of glycosylated proteins. The additional dehydration was due to concentrated sulphuric acid which at higher temperature influenced chromogen formation. On the basis of the results obtained it was concluded that, although the sensitivity of the both methods for standard fructose was comparable, TEA method was more reliable than PS method. Therefore, it is recommended in clinical practice.
PB  - Soc Medical Biochemists Yugoslavia, Belgrade
T2  - Jugoslovenska Medicinska Biohemija
T1  - Determination of serum glycosylated proteins: Comparison of thiobarbituric acid and phenol-sulphuric acid assays
VL  - 19
IS  - 4
SP  - 411
EP  - 416
UR  - https://hdl.handle.net/21.15107/rcub_cherry_445
ER  - 

@article{
author = "Mandić, Ljuba M. and Stojanović, Srđan Đ. and Colovic, A and Milin, N",
year = "2000",
abstract = "The estimation of glycosylated proteins is useful in the detection and control of long-standing hyperglycemic conditions. In this paper the content of protein-bound glucose was determined in diabetics by spectrophotometric method with phenol-sulphuric acid (PS) and with thiobarbituric acid (TBA). The amounts of protein-bound glucose obtained with the PS reagent (80.6 +/- 22.8 mmol glucose/g protein) were always considerably higher than those obtained by TEA method (3.71 +/- 1.34 mu mol glucose/g protein). The analysis was made of parameters that might have led to such significant difference. It was shown that in the reaction with PS reagent there was an additional dehydration of carbohydrate released during the hydrolysis of glycosylated proteins. The additional dehydration was due to concentrated sulphuric acid which at higher temperature influenced chromogen formation. On the basis of the results obtained it was concluded that, although the sensitivity of the both methods for standard fructose was comparable, TEA method was more reliable than PS method. Therefore, it is recommended in clinical practice.",
publisher = "Soc Medical Biochemists Yugoslavia, Belgrade",
journal = "Jugoslovenska Medicinska Biohemija",
title = "Determination of serum glycosylated proteins: Comparison of thiobarbituric acid and phenol-sulphuric acid assays",
volume = "19",
number = "4",
pages = "411-416",
url = "https://hdl.handle.net/21.15107/rcub_cherry_445"
}

Mandić, L. M., Stojanović, S. Đ., Colovic, A.,& Milin, N.. (2000). Determination of serum glycosylated proteins: Comparison of thiobarbituric acid and phenol-sulphuric acid assays. in Jugoslovenska Medicinska Biohemija
Soc Medical Biochemists Yugoslavia, Belgrade., 19(4), 411-416.
https://hdl.handle.net/21.15107/rcub_cherry_445

Mandić LM, Stojanović SĐ, Colovic A, Milin N. Determination of serum glycosylated proteins: Comparison of thiobarbituric acid and phenol-sulphuric acid assays. in Jugoslovenska Medicinska Biohemija. 2000;19(4):411-416.
https://hdl.handle.net/21.15107/rcub_cherry_445 .

Mandić, Ljuba M., Stojanović, Srđan Đ., Colovic, A, Milin, N, "Determination of serum glycosylated proteins: Comparison of thiobarbituric acid and phenol-sulphuric acid assays" in Jugoslovenska Medicinska Biohemija, 19, no. 4 (2000):411-416,
https://hdl.handle.net/21.15107/rcub_cherry_445 .