The Balancing of Peroxynitrite Detoxification between Ferric Heme-Proteins and CO<sub<2</sub<: The Case of Zebrafish Nitrobindin

Nitrobindins (Nbs) are all-β-barrel heme proteins and are present in prokaryotes and eukaryotes. Although their function(s) is still obscure, Nbs trap NO and inactivate peroxynitrite. Here, the kinetics of peroxynitrite scavenging by ferric <i<Danio rerio</i< Nb (<i<Dr</i<-Nb...
Ausführliche Beschreibung

Gespeichert in:

Autor*in:	Giovanna De Simone [verfasserIn] Andrea Coletta [verfasserIn] Alessandra di Masi [verfasserIn] Massimo Coletta [verfasserIn] Paolo Ascenzi [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2022

Schlagwörter:	effect of CO kinetics peroxynitrite detoxification tyrosine protection zebrafish nitrobindin

Übergeordnetes Werk:	In: Antioxidants - MDPI AG, 2013, 11(2022), 10, p 1932
Übergeordnetes Werk:	volume:11 ; year:2022 ; number:10, p 1932

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.3390/antiox11101932

Katalog-ID:	DOAJ027993094

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520			\|a Nitrobindins (Nbs) are all-β-barrel heme proteins and are present in prokaryotes and eukaryotes. Although their function(s) is still obscure, Nbs trap NO and inactivate peroxynitrite. Here, the kinetics of peroxynitrite scavenging by ferric <i<Danio rerio</i< Nb (<i<Dr</i<-Nb(III)) in the absence and presence of CO<sub<2</sub< is reported. The <i<Dr</i<-Nb(III)-catalyzed scavenging of peroxynitrite is facilitated by a low pH, indicating that the heme protein interacts preferentially with peroxynitrous acid, leading to the formation of nitrate (~91%) and nitrite (~9%). The physiological levels of CO<sub<2</sub< dramatically facilitate the spontaneous decay of peroxynitrite, overwhelming the scavenging activity of <i<Dr</i<-Nb(III). The effect of <i<Dr</i<-Nb(III) on the peroxynitrite-induced nitration of L-tyrosine was also investigated. <i<Dr</i<-Nb(III) inhibits the peroxynitrite-mediated nitration of free L-tyrosine, while, in the presence of CO<sub<2</sub<, <i<Dr</i<-Nb(III) does not impair nitro-L-tyrosine formation. The comparative analysis of the present results with data reported in the literature indicates that, to act as efficient peroxynitrite scavengers in vivo, i.e., in the presence of physiological levels of CO<sub<2</sub<, the ferric heme protein concentration must be higher than 10<sup<−4</sup< M. Thus, only the circulating ferric hemoglobin levels appear to be high enough to efficiently compete with CO<sub<2</sub</HCO<sub<3</sub<<sup<−</sup< in peroxynitrite inactivation. The present results are of the utmost importance for tissues, like the eye retina in fish, where blood circulation is critical for adaptation to diving conditions.
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allfields	10.3390/antiox11101932 doi (DE-627)DOAJ027993094 (DE-599)DOAJ8924a5ecb63a4e4c9892fc33efbf2e70 DE-627 ger DE-627 rakwb eng RM1-950 Giovanna De Simone verfasserin aut The Balancing of Peroxynitrite Detoxification between Ferric Heme-Proteins and CO<sub<2</sub<: The Case of Zebrafish Nitrobindin 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Nitrobindins (Nbs) are all-β-barrel heme proteins and are present in prokaryotes and eukaryotes. Although their function(s) is still obscure, Nbs trap NO and inactivate peroxynitrite. Here, the kinetics of peroxynitrite scavenging by ferric <i<Danio rerio</i< Nb (<i<Dr</i<-Nb(III)) in the absence and presence of CO<sub<2</sub< is reported. The <i<Dr</i<-Nb(III)-catalyzed scavenging of peroxynitrite is facilitated by a low pH, indicating that the heme protein interacts preferentially with peroxynitrous acid, leading to the formation of nitrate (~91%) and nitrite (~9%). The physiological levels of CO<sub<2</sub< dramatically facilitate the spontaneous decay of peroxynitrite, overwhelming the scavenging activity of <i<Dr</i<-Nb(III). The effect of <i<Dr</i<-Nb(III) on the peroxynitrite-induced nitration of L-tyrosine was also investigated. <i<Dr</i<-Nb(III) inhibits the peroxynitrite-mediated nitration of free L-tyrosine, while, in the presence of CO<sub<2</sub<, <i<Dr</i<-Nb(III) does not impair nitro-L-tyrosine formation. The comparative analysis of the present results with data reported in the literature indicates that, to act as efficient peroxynitrite scavengers in vivo, i.e., in the presence of physiological levels of CO<sub<2</sub<, the ferric heme protein concentration must be higher than 10<sup<−4</sup< M. Thus, only the circulating ferric hemoglobin levels appear to be high enough to efficiently compete with CO<sub<2</sub</HCO<sub<3</sub<<sup<−</sup< in peroxynitrite inactivation. The present results are of the utmost importance for tissues, like the eye retina in fish, where blood circulation is critical for adaptation to diving conditions. <i<Danio rerio</i< heme-protein effect of CO<sub<2</sub< kinetics peroxynitrite detoxification tyrosine protection zebrafish nitrobindin Therapeutics. Pharmacology Andrea Coletta verfasserin aut Alessandra di Masi verfasserin aut Massimo Coletta verfasserin aut Paolo Ascenzi verfasserin aut In Antioxidants MDPI AG, 2013 11(2022), 10, p 1932 (DE-627)737287578 (DE-600)2704216-9 20763921 nnns volume:11 year:2022 number:10, p 1932 https://doi.org/10.3390/antiox11101932 kostenfrei https://doaj.org/article/8924a5ecb63a4e4c9892fc33efbf2e70 kostenfrei https://www.mdpi.com/2076-3921/11/10/1932 kostenfrei https://doaj.org/toc/2076-3921 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 11 2022 10, p 1932
spelling	10.3390/antiox11101932 doi (DE-627)DOAJ027993094 (DE-599)DOAJ8924a5ecb63a4e4c9892fc33efbf2e70 DE-627 ger DE-627 rakwb eng RM1-950 Giovanna De Simone verfasserin aut The Balancing of Peroxynitrite Detoxification between Ferric Heme-Proteins and CO<sub<2</sub<: The Case of Zebrafish Nitrobindin 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Nitrobindins (Nbs) are all-β-barrel heme proteins and are present in prokaryotes and eukaryotes. Although their function(s) is still obscure, Nbs trap NO and inactivate peroxynitrite. Here, the kinetics of peroxynitrite scavenging by ferric <i<Danio rerio</i< Nb (<i<Dr</i<-Nb(III)) in the absence and presence of CO<sub<2</sub< is reported. The <i<Dr</i<-Nb(III)-catalyzed scavenging of peroxynitrite is facilitated by a low pH, indicating that the heme protein interacts preferentially with peroxynitrous acid, leading to the formation of nitrate (~91%) and nitrite (~9%). The physiological levels of CO<sub<2</sub< dramatically facilitate the spontaneous decay of peroxynitrite, overwhelming the scavenging activity of <i<Dr</i<-Nb(III). The effect of <i<Dr</i<-Nb(III) on the peroxynitrite-induced nitration of L-tyrosine was also investigated. <i<Dr</i<-Nb(III) inhibits the peroxynitrite-mediated nitration of free L-tyrosine, while, in the presence of CO<sub<2</sub<, <i<Dr</i<-Nb(III) does not impair nitro-L-tyrosine formation. The comparative analysis of the present results with data reported in the literature indicates that, to act as efficient peroxynitrite scavengers in vivo, i.e., in the presence of physiological levels of CO<sub<2</sub<, the ferric heme protein concentration must be higher than 10<sup<−4</sup< M. Thus, only the circulating ferric hemoglobin levels appear to be high enough to efficiently compete with CO<sub<2</sub</HCO<sub<3</sub<<sup<−</sup< in peroxynitrite inactivation. The present results are of the utmost importance for tissues, like the eye retina in fish, where blood circulation is critical for adaptation to diving conditions. <i<Danio rerio</i< heme-protein effect of CO<sub<2</sub< kinetics peroxynitrite detoxification tyrosine protection zebrafish nitrobindin Therapeutics. Pharmacology Andrea Coletta verfasserin aut Alessandra di Masi verfasserin aut Massimo Coletta verfasserin aut Paolo Ascenzi verfasserin aut In Antioxidants MDPI AG, 2013 11(2022), 10, p 1932 (DE-627)737287578 (DE-600)2704216-9 20763921 nnns volume:11 year:2022 number:10, p 1932 https://doi.org/10.3390/antiox11101932 kostenfrei https://doaj.org/article/8924a5ecb63a4e4c9892fc33efbf2e70 kostenfrei https://www.mdpi.com/2076-3921/11/10/1932 kostenfrei https://doaj.org/toc/2076-3921 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 11 2022 10, p 1932
allfields_unstemmed	10.3390/antiox11101932 doi (DE-627)DOAJ027993094 (DE-599)DOAJ8924a5ecb63a4e4c9892fc33efbf2e70 DE-627 ger DE-627 rakwb eng RM1-950 Giovanna De Simone verfasserin aut The Balancing of Peroxynitrite Detoxification between Ferric Heme-Proteins and CO<sub<2</sub<: The Case of Zebrafish Nitrobindin 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Nitrobindins (Nbs) are all-β-barrel heme proteins and are present in prokaryotes and eukaryotes. Although their function(s) is still obscure, Nbs trap NO and inactivate peroxynitrite. Here, the kinetics of peroxynitrite scavenging by ferric <i<Danio rerio</i< Nb (<i<Dr</i<-Nb(III)) in the absence and presence of CO<sub<2</sub< is reported. The <i<Dr</i<-Nb(III)-catalyzed scavenging of peroxynitrite is facilitated by a low pH, indicating that the heme protein interacts preferentially with peroxynitrous acid, leading to the formation of nitrate (~91%) and nitrite (~9%). The physiological levels of CO<sub<2</sub< dramatically facilitate the spontaneous decay of peroxynitrite, overwhelming the scavenging activity of <i<Dr</i<-Nb(III). The effect of <i<Dr</i<-Nb(III) on the peroxynitrite-induced nitration of L-tyrosine was also investigated. <i<Dr</i<-Nb(III) inhibits the peroxynitrite-mediated nitration of free L-tyrosine, while, in the presence of CO<sub<2</sub<, <i<Dr</i<-Nb(III) does not impair nitro-L-tyrosine formation. The comparative analysis of the present results with data reported in the literature indicates that, to act as efficient peroxynitrite scavengers in vivo, i.e., in the presence of physiological levels of CO<sub<2</sub<, the ferric heme protein concentration must be higher than 10<sup<−4</sup< M. Thus, only the circulating ferric hemoglobin levels appear to be high enough to efficiently compete with CO<sub<2</sub</HCO<sub<3</sub<<sup<−</sup< in peroxynitrite inactivation. The present results are of the utmost importance for tissues, like the eye retina in fish, where blood circulation is critical for adaptation to diving conditions. <i<Danio rerio</i< heme-protein effect of CO<sub<2</sub< kinetics peroxynitrite detoxification tyrosine protection zebrafish nitrobindin Therapeutics. Pharmacology Andrea Coletta verfasserin aut Alessandra di Masi verfasserin aut Massimo Coletta verfasserin aut Paolo Ascenzi verfasserin aut In Antioxidants MDPI AG, 2013 11(2022), 10, p 1932 (DE-627)737287578 (DE-600)2704216-9 20763921 nnns volume:11 year:2022 number:10, p 1932 https://doi.org/10.3390/antiox11101932 kostenfrei https://doaj.org/article/8924a5ecb63a4e4c9892fc33efbf2e70 kostenfrei https://www.mdpi.com/2076-3921/11/10/1932 kostenfrei https://doaj.org/toc/2076-3921 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 11 2022 10, p 1932
allfieldsGer	10.3390/antiox11101932 doi (DE-627)DOAJ027993094 (DE-599)DOAJ8924a5ecb63a4e4c9892fc33efbf2e70 DE-627 ger DE-627 rakwb eng RM1-950 Giovanna De Simone verfasserin aut The Balancing of Peroxynitrite Detoxification between Ferric Heme-Proteins and CO<sub<2</sub<: The Case of Zebrafish Nitrobindin 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Nitrobindins (Nbs) are all-β-barrel heme proteins and are present in prokaryotes and eukaryotes. Although their function(s) is still obscure, Nbs trap NO and inactivate peroxynitrite. Here, the kinetics of peroxynitrite scavenging by ferric <i<Danio rerio</i< Nb (<i<Dr</i<-Nb(III)) in the absence and presence of CO<sub<2</sub< is reported. The <i<Dr</i<-Nb(III)-catalyzed scavenging of peroxynitrite is facilitated by a low pH, indicating that the heme protein interacts preferentially with peroxynitrous acid, leading to the formation of nitrate (~91%) and nitrite (~9%). The physiological levels of CO<sub<2</sub< dramatically facilitate the spontaneous decay of peroxynitrite, overwhelming the scavenging activity of <i<Dr</i<-Nb(III). The effect of <i<Dr</i<-Nb(III) on the peroxynitrite-induced nitration of L-tyrosine was also investigated. <i<Dr</i<-Nb(III) inhibits the peroxynitrite-mediated nitration of free L-tyrosine, while, in the presence of CO<sub<2</sub<, <i<Dr</i<-Nb(III) does not impair nitro-L-tyrosine formation. The comparative analysis of the present results with data reported in the literature indicates that, to act as efficient peroxynitrite scavengers in vivo, i.e., in the presence of physiological levels of CO<sub<2</sub<, the ferric heme protein concentration must be higher than 10<sup<−4</sup< M. Thus, only the circulating ferric hemoglobin levels appear to be high enough to efficiently compete with CO<sub<2</sub</HCO<sub<3</sub<<sup<−</sup< in peroxynitrite inactivation. The present results are of the utmost importance for tissues, like the eye retina in fish, where blood circulation is critical for adaptation to diving conditions. <i<Danio rerio</i< heme-protein effect of CO<sub<2</sub< kinetics peroxynitrite detoxification tyrosine protection zebrafish nitrobindin Therapeutics. Pharmacology Andrea Coletta verfasserin aut Alessandra di Masi verfasserin aut Massimo Coletta verfasserin aut Paolo Ascenzi verfasserin aut In Antioxidants MDPI AG, 2013 11(2022), 10, p 1932 (DE-627)737287578 (DE-600)2704216-9 20763921 nnns volume:11 year:2022 number:10, p 1932 https://doi.org/10.3390/antiox11101932 kostenfrei https://doaj.org/article/8924a5ecb63a4e4c9892fc33efbf2e70 kostenfrei https://www.mdpi.com/2076-3921/11/10/1932 kostenfrei https://doaj.org/toc/2076-3921 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 11 2022 10, p 1932
allfieldsSound	10.3390/antiox11101932 doi (DE-627)DOAJ027993094 (DE-599)DOAJ8924a5ecb63a4e4c9892fc33efbf2e70 DE-627 ger DE-627 rakwb eng RM1-950 Giovanna De Simone verfasserin aut The Balancing of Peroxynitrite Detoxification between Ferric Heme-Proteins and CO<sub<2</sub<: The Case of Zebrafish Nitrobindin 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Nitrobindins (Nbs) are all-β-barrel heme proteins and are present in prokaryotes and eukaryotes. Although their function(s) is still obscure, Nbs trap NO and inactivate peroxynitrite. Here, the kinetics of peroxynitrite scavenging by ferric <i<Danio rerio</i< Nb (<i<Dr</i<-Nb(III)) in the absence and presence of CO<sub<2</sub< is reported. The <i<Dr</i<-Nb(III)-catalyzed scavenging of peroxynitrite is facilitated by a low pH, indicating that the heme protein interacts preferentially with peroxynitrous acid, leading to the formation of nitrate (~91%) and nitrite (~9%). The physiological levels of CO<sub<2</sub< dramatically facilitate the spontaneous decay of peroxynitrite, overwhelming the scavenging activity of <i<Dr</i<-Nb(III). The effect of <i<Dr</i<-Nb(III) on the peroxynitrite-induced nitration of L-tyrosine was also investigated. <i<Dr</i<-Nb(III) inhibits the peroxynitrite-mediated nitration of free L-tyrosine, while, in the presence of CO<sub<2</sub<, <i<Dr</i<-Nb(III) does not impair nitro-L-tyrosine formation. The comparative analysis of the present results with data reported in the literature indicates that, to act as efficient peroxynitrite scavengers in vivo, i.e., in the presence of physiological levels of CO<sub<2</sub<, the ferric heme protein concentration must be higher than 10<sup<−4</sup< M. Thus, only the circulating ferric hemoglobin levels appear to be high enough to efficiently compete with CO<sub<2</sub</HCO<sub<3</sub<<sup<−</sup< in peroxynitrite inactivation. The present results are of the utmost importance for tissues, like the eye retina in fish, where blood circulation is critical for adaptation to diving conditions. <i<Danio rerio</i< heme-protein effect of CO<sub<2</sub< kinetics peroxynitrite detoxification tyrosine protection zebrafish nitrobindin Therapeutics. Pharmacology Andrea Coletta verfasserin aut Alessandra di Masi verfasserin aut Massimo Coletta verfasserin aut Paolo Ascenzi verfasserin aut In Antioxidants MDPI AG, 2013 11(2022), 10, p 1932 (DE-627)737287578 (DE-600)2704216-9 20763921 nnns volume:11 year:2022 number:10, p 1932 https://doi.org/10.3390/antiox11101932 kostenfrei https://doaj.org/article/8924a5ecb63a4e4c9892fc33efbf2e70 kostenfrei https://www.mdpi.com/2076-3921/11/10/1932 kostenfrei https://doaj.org/toc/2076-3921 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 11 2022 10, p 1932
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source	In Antioxidants 11(2022), 10, p 1932 volume:11 year:2022 number:10, p 1932
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topic_facet	<i<Danio rerio</i< heme-protein effect of CO<sub<2</sub< kinetics peroxynitrite detoxification tyrosine protection zebrafish nitrobindin Therapeutics. Pharmacology
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author	Giovanna De Simone
spellingShingle	Giovanna De Simone misc RM1-950 misc <i<Danio rerio</i< heme-protein misc effect of CO<sub<2</sub< misc kinetics misc peroxynitrite detoxification misc tyrosine protection misc zebrafish nitrobindin misc Therapeutics. Pharmacology The Balancing of Peroxynitrite Detoxification between Ferric Heme-Proteins and CO<sub<2</sub<: The Case of Zebrafish Nitrobindin
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topic_title	RM1-950 The Balancing of Peroxynitrite Detoxification between Ferric Heme-Proteins and CO<sub<2</sub<: The Case of Zebrafish Nitrobindin <i<Danio rerio</i< heme-protein effect of CO<sub<2</sub< kinetics peroxynitrite detoxification tyrosine protection zebrafish nitrobindin
topic	misc RM1-950 misc <i<Danio rerio</i< heme-protein misc effect of CO<sub<2</sub< misc kinetics misc peroxynitrite detoxification misc tyrosine protection misc zebrafish nitrobindin misc Therapeutics. Pharmacology
topic_unstemmed	misc RM1-950 misc <i<Danio rerio</i< heme-protein misc effect of CO<sub<2</sub< misc kinetics misc peroxynitrite detoxification misc tyrosine protection misc zebrafish nitrobindin misc Therapeutics. Pharmacology
topic_browse	misc RM1-950 misc <i<Danio rerio</i< heme-protein misc effect of CO<sub<2</sub< misc kinetics misc peroxynitrite detoxification misc tyrosine protection misc zebrafish nitrobindin misc Therapeutics. Pharmacology
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hierarchy_parent_title	Antioxidants
hierarchy_parent_id	737287578
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title	The Balancing of Peroxynitrite Detoxification between Ferric Heme-Proteins and CO<sub<2</sub<: The Case of Zebrafish Nitrobindin
ctrlnum	(DE-627)DOAJ027993094 (DE-599)DOAJ8924a5ecb63a4e4c9892fc33efbf2e70
title_full	The Balancing of Peroxynitrite Detoxification between Ferric Heme-Proteins and CO<sub<2</sub<: The Case of Zebrafish Nitrobindin
author_sort	Giovanna De Simone
journal	Antioxidants
journalStr	Antioxidants
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lang_code	eng
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publishDateSort	2022
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author_browse	Giovanna De Simone Andrea Coletta Alessandra di Masi Massimo Coletta Paolo Ascenzi
container_volume	11
class	RM1-950
format_se	Elektronische Aufsätze
author-letter	Giovanna De Simone
doi_str_mv	10.3390/antiox11101932
author2-role	verfasserin
title_sort	balancing of peroxynitrite detoxification between ferric heme-proteins and co<sub<2</sub<: the case of zebrafish nitrobindin
callnumber	RM1-950
title_auth	The Balancing of Peroxynitrite Detoxification between Ferric Heme-Proteins and CO<sub<2</sub<: The Case of Zebrafish Nitrobindin
abstract	Nitrobindins (Nbs) are all-β-barrel heme proteins and are present in prokaryotes and eukaryotes. Although their function(s) is still obscure, Nbs trap NO and inactivate peroxynitrite. Here, the kinetics of peroxynitrite scavenging by ferric <i<Danio rerio</i< Nb (<i<Dr</i<-Nb(III)) in the absence and presence of CO<sub<2</sub< is reported. The <i<Dr</i<-Nb(III)-catalyzed scavenging of peroxynitrite is facilitated by a low pH, indicating that the heme protein interacts preferentially with peroxynitrous acid, leading to the formation of nitrate (~91%) and nitrite (~9%). The physiological levels of CO<sub<2</sub< dramatically facilitate the spontaneous decay of peroxynitrite, overwhelming the scavenging activity of <i<Dr</i<-Nb(III). The effect of <i<Dr</i<-Nb(III) on the peroxynitrite-induced nitration of L-tyrosine was also investigated. <i<Dr</i<-Nb(III) inhibits the peroxynitrite-mediated nitration of free L-tyrosine, while, in the presence of CO<sub<2</sub<, <i<Dr</i<-Nb(III) does not impair nitro-L-tyrosine formation. The comparative analysis of the present results with data reported in the literature indicates that, to act as efficient peroxynitrite scavengers in vivo, i.e., in the presence of physiological levels of CO<sub<2</sub<, the ferric heme protein concentration must be higher than 10<sup<−4</sup< M. Thus, only the circulating ferric hemoglobin levels appear to be high enough to efficiently compete with CO<sub<2</sub</HCO<sub<3</sub<<sup<−</sup< in peroxynitrite inactivation. The present results are of the utmost importance for tissues, like the eye retina in fish, where blood circulation is critical for adaptation to diving conditions.
abstractGer	Nitrobindins (Nbs) are all-β-barrel heme proteins and are present in prokaryotes and eukaryotes. Although their function(s) is still obscure, Nbs trap NO and inactivate peroxynitrite. Here, the kinetics of peroxynitrite scavenging by ferric <i<Danio rerio</i< Nb (<i<Dr</i<-Nb(III)) in the absence and presence of CO<sub<2</sub< is reported. The <i<Dr</i<-Nb(III)-catalyzed scavenging of peroxynitrite is facilitated by a low pH, indicating that the heme protein interacts preferentially with peroxynitrous acid, leading to the formation of nitrate (~91%) and nitrite (~9%). The physiological levels of CO<sub<2</sub< dramatically facilitate the spontaneous decay of peroxynitrite, overwhelming the scavenging activity of <i<Dr</i<-Nb(III). The effect of <i<Dr</i<-Nb(III) on the peroxynitrite-induced nitration of L-tyrosine was also investigated. <i<Dr</i<-Nb(III) inhibits the peroxynitrite-mediated nitration of free L-tyrosine, while, in the presence of CO<sub<2</sub<, <i<Dr</i<-Nb(III) does not impair nitro-L-tyrosine formation. The comparative analysis of the present results with data reported in the literature indicates that, to act as efficient peroxynitrite scavengers in vivo, i.e., in the presence of physiological levels of CO<sub<2</sub<, the ferric heme protein concentration must be higher than 10<sup<−4</sup< M. Thus, only the circulating ferric hemoglobin levels appear to be high enough to efficiently compete with CO<sub<2</sub</HCO<sub<3</sub<<sup<−</sup< in peroxynitrite inactivation. The present results are of the utmost importance for tissues, like the eye retina in fish, where blood circulation is critical for adaptation to diving conditions.
abstract_unstemmed	Nitrobindins (Nbs) are all-β-barrel heme proteins and are present in prokaryotes and eukaryotes. Although their function(s) is still obscure, Nbs trap NO and inactivate peroxynitrite. Here, the kinetics of peroxynitrite scavenging by ferric <i<Danio rerio</i< Nb (<i<Dr</i<-Nb(III)) in the absence and presence of CO<sub<2</sub< is reported. The <i<Dr</i<-Nb(III)-catalyzed scavenging of peroxynitrite is facilitated by a low pH, indicating that the heme protein interacts preferentially with peroxynitrous acid, leading to the formation of nitrate (~91%) and nitrite (~9%). The physiological levels of CO<sub<2</sub< dramatically facilitate the spontaneous decay of peroxynitrite, overwhelming the scavenging activity of <i<Dr</i<-Nb(III). The effect of <i<Dr</i<-Nb(III) on the peroxynitrite-induced nitration of L-tyrosine was also investigated. <i<Dr</i<-Nb(III) inhibits the peroxynitrite-mediated nitration of free L-tyrosine, while, in the presence of CO<sub<2</sub<, <i<Dr</i<-Nb(III) does not impair nitro-L-tyrosine formation. The comparative analysis of the present results with data reported in the literature indicates that, to act as efficient peroxynitrite scavengers in vivo, i.e., in the presence of physiological levels of CO<sub<2</sub<, the ferric heme protein concentration must be higher than 10<sup<−4</sup< M. Thus, only the circulating ferric hemoglobin levels appear to be high enough to efficiently compete with CO<sub<2</sub</HCO<sub<3</sub<<sup<−</sup< in peroxynitrite inactivation. The present results are of the utmost importance for tissues, like the eye retina in fish, where blood circulation is critical for adaptation to diving conditions.
collection_details	GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700
container_issue	10, p 1932
title_short	The Balancing of Peroxynitrite Detoxification between Ferric Heme-Proteins and CO<sub<2</sub<: The Case of Zebrafish Nitrobindin
url	https://doi.org/10.3390/antiox11101932 https://doaj.org/article/8924a5ecb63a4e4c9892fc33efbf2e70 https://www.mdpi.com/2076-3921/11/10/1932 https://doaj.org/toc/2076-3921
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author2	Andrea Coletta Alessandra di Masi Massimo Coletta Paolo Ascenzi
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up_date	2024-07-03T15:08:42.850Z
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