Selenocysteine oxidation in glutathione peroxidase catalysis: an MS-supported quantum mechanics study
Glutathione peroxidases (GPxs) are enzymes working with either selenium or sulfur catalysis. They adopted diverse functions ranging from detoxification of H2O2 to redox signaling and differentiation. The relative stability of the selenoenzymes, however, remained enigmatic in view of the postulated i...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Orian, Laura [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2015transfer abstract |
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| Schlagwörter: |
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| Umfang: |
14 |
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| Übergeordnetes Werk: |
Enthalten in: New organic dyes with varied arylamine donors as effective co-sensitizers for ruthenium complex N719 in dye sensitized solar cells - Wu, Zhi-Sheng ELSEVIER, 2020, the official journal of the Oxygen Society, a constituent member of the International Society for Free Radical Research, New York, NY [u.a.] |
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| Übergeordnetes Werk: |
volume:87 ; year:2015 ; pages:1-14 ; extent:14 |
| Links: |
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| DOI / URN: |
10.1016/j.freeradbiomed.2015.06.011 |
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ELV018655882 |
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| 245 | 1 | 0 | |a Selenocysteine oxidation in glutathione peroxidase catalysis: an MS-supported quantum mechanics study |
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| 520 | |a Glutathione peroxidases (GPxs) are enzymes working with either selenium or sulfur catalysis. They adopted diverse functions ranging from detoxification of H2O2 to redox signaling and differentiation. The relative stability of the selenoenzymes, however, remained enigmatic in view of the postulated involvement of a highly unstable selenenic acid form during catalysis. Nevertheless, density functional theory calculations obtained with a representative active site model verify the mechanistic concept of GPx catalysis and underscore its efficiency. However, they also allow that the selenenic acid, in the absence of the reducing substrate, reacts with a nitrogen in the active site. MS/MS analysis of oxidized rat GPx4 complies with the predicted structure, an 8-membered ring, in which selenium is bound as selenenylamide to the protein backbone. The intermediate can be re-integrated into the canonical GPx cycle by glutathione, whereas, under denaturing conditions, its selenium moiety undergoes β-cleavage with formation of a dehydro-alanine residue. The selenenylamide bypass prevents destruction of the redox center due to over-oxidation of the selenium or its elimination and likely allows fine-tuning of GPx activity or alternate substrate reactions for regulatory purposes. | ||
| 520 | |a Glutathione peroxidases (GPxs) are enzymes working with either selenium or sulfur catalysis. They adopted diverse functions ranging from detoxification of H2O2 to redox signaling and differentiation. The relative stability of the selenoenzymes, however, remained enigmatic in view of the postulated involvement of a highly unstable selenenic acid form during catalysis. Nevertheless, density functional theory calculations obtained with a representative active site model verify the mechanistic concept of GPx catalysis and underscore its efficiency. However, they also allow that the selenenic acid, in the absence of the reducing substrate, reacts with a nitrogen in the active site. MS/MS analysis of oxidized rat GPx4 complies with the predicted structure, an 8-membered ring, in which selenium is bound as selenenylamide to the protein backbone. The intermediate can be re-integrated into the canonical GPx cycle by glutathione, whereas, under denaturing conditions, its selenium moiety undergoes β-cleavage with formation of a dehydro-alanine residue. The selenenylamide bypass prevents destruction of the redox center due to over-oxidation of the selenium or its elimination and likely allows fine-tuning of GPx activity or alternate substrate reactions for regulatory purposes. | ||
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10.1016/j.freeradbiomed.2015.06.011 doi GBVA2015015000027.pica (DE-627)ELV018655882 (ELSEVIER)S0891-5849(15)00279-8 DE-627 ger DE-627 rakwb eng 570 610 570 DE-600 610 DE-600 620 VZ 52.57 bkl 53.36 bkl Orian, Laura verfasserin aut Selenocysteine oxidation in glutathione peroxidase catalysis: an MS-supported quantum mechanics study 2015transfer abstract 14 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Glutathione peroxidases (GPxs) are enzymes working with either selenium or sulfur catalysis. They adopted diverse functions ranging from detoxification of H2O2 to redox signaling and differentiation. The relative stability of the selenoenzymes, however, remained enigmatic in view of the postulated involvement of a highly unstable selenenic acid form during catalysis. Nevertheless, density functional theory calculations obtained with a representative active site model verify the mechanistic concept of GPx catalysis and underscore its efficiency. However, they also allow that the selenenic acid, in the absence of the reducing substrate, reacts with a nitrogen in the active site. MS/MS analysis of oxidized rat GPx4 complies with the predicted structure, an 8-membered ring, in which selenium is bound as selenenylamide to the protein backbone. The intermediate can be re-integrated into the canonical GPx cycle by glutathione, whereas, under denaturing conditions, its selenium moiety undergoes β-cleavage with formation of a dehydro-alanine residue. The selenenylamide bypass prevents destruction of the redox center due to over-oxidation of the selenium or its elimination and likely allows fine-tuning of GPx activity or alternate substrate reactions for regulatory purposes. Glutathione peroxidases (GPxs) are enzymes working with either selenium or sulfur catalysis. They adopted diverse functions ranging from detoxification of H2O2 to redox signaling and differentiation. The relative stability of the selenoenzymes, however, remained enigmatic in view of the postulated involvement of a highly unstable selenenic acid form during catalysis. Nevertheless, density functional theory calculations obtained with a representative active site model verify the mechanistic concept of GPx catalysis and underscore its efficiency. However, they also allow that the selenenic acid, in the absence of the reducing substrate, reacts with a nitrogen in the active site. MS/MS analysis of oxidized rat GPx4 complies with the predicted structure, an 8-membered ring, in which selenium is bound as selenenylamide to the protein backbone. The intermediate can be re-integrated into the canonical GPx cycle by glutathione, whereas, under denaturing conditions, its selenium moiety undergoes β-cleavage with formation of a dehydro-alanine residue. The selenenylamide bypass prevents destruction of the redox center due to over-oxidation of the selenium or its elimination and likely allows fine-tuning of GPx activity or alternate substrate reactions for regulatory purposes. SecGPx Elsevier GPx1 Elsevier GPx4 Elsevier CysGPx(s) Elsevier CR Elsevier PC-OOH Elsevier NF-κB Elsevier 1-CysGPx(s) Elsevier MS1 Elsevier MS/MS Elsevier LC-ESI MS/MS Elsevier LC-MS/MS Elsevier DFT Elsevier CP Elsevier U Elsevier ESI Elsevier GSH Elsevier HPLC Elsevier CID Elsevier Q-TOF Elsevier MS Elsevier GPx(s) Elsevier GPx4U46C Elsevier RMSD Elsevier 2-CysGPx(s) Elsevier CS Elsevier RrGPx4 Elsevier Sec Elsevier LC-MS Elsevier Dha Elsevier TS Elsevier Mauri, Pierluigi oth Roveri, Antonella oth Toppo, Stefano oth Benazzi, Louise oth Bosello-Travain, Valentina oth De Palma, Antonella oth Maiorino, Matilde oth Miotto, Giovanni oth Zaccarin, Mattia oth Polimeno, Antonino oth Flohé, Leopold oth Ursini, Fulvio oth Enthalten in Elsevier Wu, Zhi-Sheng ELSEVIER New organic dyes with varied arylamine donors as effective co-sensitizers for ruthenium complex N719 in dye sensitized solar cells 2020 the official journal of the Oxygen Society, a constituent member of the International Society for Free Radical Research New York, NY [u.a.] (DE-627)ELV003689417 volume:87 year:2015 pages:1-14 extent:14 https://doi.org/10.1016/j.freeradbiomed.2015.06.011 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 52.57 Energiespeicherung VZ 53.36 Energiedirektumwandler elektrische Energiespeicher VZ AR 87 2015 1-14 14 045F 570 |
| spelling |
10.1016/j.freeradbiomed.2015.06.011 doi GBVA2015015000027.pica (DE-627)ELV018655882 (ELSEVIER)S0891-5849(15)00279-8 DE-627 ger DE-627 rakwb eng 570 610 570 DE-600 610 DE-600 620 VZ 52.57 bkl 53.36 bkl Orian, Laura verfasserin aut Selenocysteine oxidation in glutathione peroxidase catalysis: an MS-supported quantum mechanics study 2015transfer abstract 14 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Glutathione peroxidases (GPxs) are enzymes working with either selenium or sulfur catalysis. They adopted diverse functions ranging from detoxification of H2O2 to redox signaling and differentiation. The relative stability of the selenoenzymes, however, remained enigmatic in view of the postulated involvement of a highly unstable selenenic acid form during catalysis. Nevertheless, density functional theory calculations obtained with a representative active site model verify the mechanistic concept of GPx catalysis and underscore its efficiency. However, they also allow that the selenenic acid, in the absence of the reducing substrate, reacts with a nitrogen in the active site. MS/MS analysis of oxidized rat GPx4 complies with the predicted structure, an 8-membered ring, in which selenium is bound as selenenylamide to the protein backbone. The intermediate can be re-integrated into the canonical GPx cycle by glutathione, whereas, under denaturing conditions, its selenium moiety undergoes β-cleavage with formation of a dehydro-alanine residue. The selenenylamide bypass prevents destruction of the redox center due to over-oxidation of the selenium or its elimination and likely allows fine-tuning of GPx activity or alternate substrate reactions for regulatory purposes. Glutathione peroxidases (GPxs) are enzymes working with either selenium or sulfur catalysis. They adopted diverse functions ranging from detoxification of H2O2 to redox signaling and differentiation. The relative stability of the selenoenzymes, however, remained enigmatic in view of the postulated involvement of a highly unstable selenenic acid form during catalysis. Nevertheless, density functional theory calculations obtained with a representative active site model verify the mechanistic concept of GPx catalysis and underscore its efficiency. However, they also allow that the selenenic acid, in the absence of the reducing substrate, reacts with a nitrogen in the active site. MS/MS analysis of oxidized rat GPx4 complies with the predicted structure, an 8-membered ring, in which selenium is bound as selenenylamide to the protein backbone. The intermediate can be re-integrated into the canonical GPx cycle by glutathione, whereas, under denaturing conditions, its selenium moiety undergoes β-cleavage with formation of a dehydro-alanine residue. The selenenylamide bypass prevents destruction of the redox center due to over-oxidation of the selenium or its elimination and likely allows fine-tuning of GPx activity or alternate substrate reactions for regulatory purposes. SecGPx Elsevier GPx1 Elsevier GPx4 Elsevier CysGPx(s) Elsevier CR Elsevier PC-OOH Elsevier NF-κB Elsevier 1-CysGPx(s) Elsevier MS1 Elsevier MS/MS Elsevier LC-ESI MS/MS Elsevier LC-MS/MS Elsevier DFT Elsevier CP Elsevier U Elsevier ESI Elsevier GSH Elsevier HPLC Elsevier CID Elsevier Q-TOF Elsevier MS Elsevier GPx(s) Elsevier GPx4U46C Elsevier RMSD Elsevier 2-CysGPx(s) Elsevier CS Elsevier RrGPx4 Elsevier Sec Elsevier LC-MS Elsevier Dha Elsevier TS Elsevier Mauri, Pierluigi oth Roveri, Antonella oth Toppo, Stefano oth Benazzi, Louise oth Bosello-Travain, Valentina oth De Palma, Antonella oth Maiorino, Matilde oth Miotto, Giovanni oth Zaccarin, Mattia oth Polimeno, Antonino oth Flohé, Leopold oth Ursini, Fulvio oth Enthalten in Elsevier Wu, Zhi-Sheng ELSEVIER New organic dyes with varied arylamine donors as effective co-sensitizers for ruthenium complex N719 in dye sensitized solar cells 2020 the official journal of the Oxygen Society, a constituent member of the International Society for Free Radical Research New York, NY [u.a.] (DE-627)ELV003689417 volume:87 year:2015 pages:1-14 extent:14 https://doi.org/10.1016/j.freeradbiomed.2015.06.011 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 52.57 Energiespeicherung VZ 53.36 Energiedirektumwandler elektrische Energiespeicher VZ AR 87 2015 1-14 14 045F 570 |
| allfields_unstemmed |
10.1016/j.freeradbiomed.2015.06.011 doi GBVA2015015000027.pica (DE-627)ELV018655882 (ELSEVIER)S0891-5849(15)00279-8 DE-627 ger DE-627 rakwb eng 570 610 570 DE-600 610 DE-600 620 VZ 52.57 bkl 53.36 bkl Orian, Laura verfasserin aut Selenocysteine oxidation in glutathione peroxidase catalysis: an MS-supported quantum mechanics study 2015transfer abstract 14 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Glutathione peroxidases (GPxs) are enzymes working with either selenium or sulfur catalysis. They adopted diverse functions ranging from detoxification of H2O2 to redox signaling and differentiation. The relative stability of the selenoenzymes, however, remained enigmatic in view of the postulated involvement of a highly unstable selenenic acid form during catalysis. Nevertheless, density functional theory calculations obtained with a representative active site model verify the mechanistic concept of GPx catalysis and underscore its efficiency. However, they also allow that the selenenic acid, in the absence of the reducing substrate, reacts with a nitrogen in the active site. MS/MS analysis of oxidized rat GPx4 complies with the predicted structure, an 8-membered ring, in which selenium is bound as selenenylamide to the protein backbone. The intermediate can be re-integrated into the canonical GPx cycle by glutathione, whereas, under denaturing conditions, its selenium moiety undergoes β-cleavage with formation of a dehydro-alanine residue. The selenenylamide bypass prevents destruction of the redox center due to over-oxidation of the selenium or its elimination and likely allows fine-tuning of GPx activity or alternate substrate reactions for regulatory purposes. Glutathione peroxidases (GPxs) are enzymes working with either selenium or sulfur catalysis. They adopted diverse functions ranging from detoxification of H2O2 to redox signaling and differentiation. The relative stability of the selenoenzymes, however, remained enigmatic in view of the postulated involvement of a highly unstable selenenic acid form during catalysis. Nevertheless, density functional theory calculations obtained with a representative active site model verify the mechanistic concept of GPx catalysis and underscore its efficiency. However, they also allow that the selenenic acid, in the absence of the reducing substrate, reacts with a nitrogen in the active site. MS/MS analysis of oxidized rat GPx4 complies with the predicted structure, an 8-membered ring, in which selenium is bound as selenenylamide to the protein backbone. The intermediate can be re-integrated into the canonical GPx cycle by glutathione, whereas, under denaturing conditions, its selenium moiety undergoes β-cleavage with formation of a dehydro-alanine residue. The selenenylamide bypass prevents destruction of the redox center due to over-oxidation of the selenium or its elimination and likely allows fine-tuning of GPx activity or alternate substrate reactions for regulatory purposes. SecGPx Elsevier GPx1 Elsevier GPx4 Elsevier CysGPx(s) Elsevier CR Elsevier PC-OOH Elsevier NF-κB Elsevier 1-CysGPx(s) Elsevier MS1 Elsevier MS/MS Elsevier LC-ESI MS/MS Elsevier LC-MS/MS Elsevier DFT Elsevier CP Elsevier U Elsevier ESI Elsevier GSH Elsevier HPLC Elsevier CID Elsevier Q-TOF Elsevier MS Elsevier GPx(s) Elsevier GPx4U46C Elsevier RMSD Elsevier 2-CysGPx(s) Elsevier CS Elsevier RrGPx4 Elsevier Sec Elsevier LC-MS Elsevier Dha Elsevier TS Elsevier Mauri, Pierluigi oth Roveri, Antonella oth Toppo, Stefano oth Benazzi, Louise oth Bosello-Travain, Valentina oth De Palma, Antonella oth Maiorino, Matilde oth Miotto, Giovanni oth Zaccarin, Mattia oth Polimeno, Antonino oth Flohé, Leopold oth Ursini, Fulvio oth Enthalten in Elsevier Wu, Zhi-Sheng ELSEVIER New organic dyes with varied arylamine donors as effective co-sensitizers for ruthenium complex N719 in dye sensitized solar cells 2020 the official journal of the Oxygen Society, a constituent member of the International Society for Free Radical Research New York, NY [u.a.] (DE-627)ELV003689417 volume:87 year:2015 pages:1-14 extent:14 https://doi.org/10.1016/j.freeradbiomed.2015.06.011 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 52.57 Energiespeicherung VZ 53.36 Energiedirektumwandler elektrische Energiespeicher VZ AR 87 2015 1-14 14 045F 570 |
| allfieldsGer |
10.1016/j.freeradbiomed.2015.06.011 doi GBVA2015015000027.pica (DE-627)ELV018655882 (ELSEVIER)S0891-5849(15)00279-8 DE-627 ger DE-627 rakwb eng 570 610 570 DE-600 610 DE-600 620 VZ 52.57 bkl 53.36 bkl Orian, Laura verfasserin aut Selenocysteine oxidation in glutathione peroxidase catalysis: an MS-supported quantum mechanics study 2015transfer abstract 14 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Glutathione peroxidases (GPxs) are enzymes working with either selenium or sulfur catalysis. They adopted diverse functions ranging from detoxification of H2O2 to redox signaling and differentiation. The relative stability of the selenoenzymes, however, remained enigmatic in view of the postulated involvement of a highly unstable selenenic acid form during catalysis. Nevertheless, density functional theory calculations obtained with a representative active site model verify the mechanistic concept of GPx catalysis and underscore its efficiency. However, they also allow that the selenenic acid, in the absence of the reducing substrate, reacts with a nitrogen in the active site. MS/MS analysis of oxidized rat GPx4 complies with the predicted structure, an 8-membered ring, in which selenium is bound as selenenylamide to the protein backbone. The intermediate can be re-integrated into the canonical GPx cycle by glutathione, whereas, under denaturing conditions, its selenium moiety undergoes β-cleavage with formation of a dehydro-alanine residue. The selenenylamide bypass prevents destruction of the redox center due to over-oxidation of the selenium or its elimination and likely allows fine-tuning of GPx activity or alternate substrate reactions for regulatory purposes. Glutathione peroxidases (GPxs) are enzymes working with either selenium or sulfur catalysis. They adopted diverse functions ranging from detoxification of H2O2 to redox signaling and differentiation. The relative stability of the selenoenzymes, however, remained enigmatic in view of the postulated involvement of a highly unstable selenenic acid form during catalysis. Nevertheless, density functional theory calculations obtained with a representative active site model verify the mechanistic concept of GPx catalysis and underscore its efficiency. However, they also allow that the selenenic acid, in the absence of the reducing substrate, reacts with a nitrogen in the active site. MS/MS analysis of oxidized rat GPx4 complies with the predicted structure, an 8-membered ring, in which selenium is bound as selenenylamide to the protein backbone. The intermediate can be re-integrated into the canonical GPx cycle by glutathione, whereas, under denaturing conditions, its selenium moiety undergoes β-cleavage with formation of a dehydro-alanine residue. The selenenylamide bypass prevents destruction of the redox center due to over-oxidation of the selenium or its elimination and likely allows fine-tuning of GPx activity or alternate substrate reactions for regulatory purposes. SecGPx Elsevier GPx1 Elsevier GPx4 Elsevier CysGPx(s) Elsevier CR Elsevier PC-OOH Elsevier NF-κB Elsevier 1-CysGPx(s) Elsevier MS1 Elsevier MS/MS Elsevier LC-ESI MS/MS Elsevier LC-MS/MS Elsevier DFT Elsevier CP Elsevier U Elsevier ESI Elsevier GSH Elsevier HPLC Elsevier CID Elsevier Q-TOF Elsevier MS Elsevier GPx(s) Elsevier GPx4U46C Elsevier RMSD Elsevier 2-CysGPx(s) Elsevier CS Elsevier RrGPx4 Elsevier Sec Elsevier LC-MS Elsevier Dha Elsevier TS Elsevier Mauri, Pierluigi oth Roveri, Antonella oth Toppo, Stefano oth Benazzi, Louise oth Bosello-Travain, Valentina oth De Palma, Antonella oth Maiorino, Matilde oth Miotto, Giovanni oth Zaccarin, Mattia oth Polimeno, Antonino oth Flohé, Leopold oth Ursini, Fulvio oth Enthalten in Elsevier Wu, Zhi-Sheng ELSEVIER New organic dyes with varied arylamine donors as effective co-sensitizers for ruthenium complex N719 in dye sensitized solar cells 2020 the official journal of the Oxygen Society, a constituent member of the International Society for Free Radical Research New York, NY [u.a.] (DE-627)ELV003689417 volume:87 year:2015 pages:1-14 extent:14 https://doi.org/10.1016/j.freeradbiomed.2015.06.011 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 52.57 Energiespeicherung VZ 53.36 Energiedirektumwandler elektrische Energiespeicher VZ AR 87 2015 1-14 14 045F 570 |
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10.1016/j.freeradbiomed.2015.06.011 doi GBVA2015015000027.pica (DE-627)ELV018655882 (ELSEVIER)S0891-5849(15)00279-8 DE-627 ger DE-627 rakwb eng 570 610 570 DE-600 610 DE-600 620 VZ 52.57 bkl 53.36 bkl Orian, Laura verfasserin aut Selenocysteine oxidation in glutathione peroxidase catalysis: an MS-supported quantum mechanics study 2015transfer abstract 14 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Glutathione peroxidases (GPxs) are enzymes working with either selenium or sulfur catalysis. They adopted diverse functions ranging from detoxification of H2O2 to redox signaling and differentiation. The relative stability of the selenoenzymes, however, remained enigmatic in view of the postulated involvement of a highly unstable selenenic acid form during catalysis. Nevertheless, density functional theory calculations obtained with a representative active site model verify the mechanistic concept of GPx catalysis and underscore its efficiency. However, they also allow that the selenenic acid, in the absence of the reducing substrate, reacts with a nitrogen in the active site. MS/MS analysis of oxidized rat GPx4 complies with the predicted structure, an 8-membered ring, in which selenium is bound as selenenylamide to the protein backbone. The intermediate can be re-integrated into the canonical GPx cycle by glutathione, whereas, under denaturing conditions, its selenium moiety undergoes β-cleavage with formation of a dehydro-alanine residue. The selenenylamide bypass prevents destruction of the redox center due to over-oxidation of the selenium or its elimination and likely allows fine-tuning of GPx activity or alternate substrate reactions for regulatory purposes. Glutathione peroxidases (GPxs) are enzymes working with either selenium or sulfur catalysis. They adopted diverse functions ranging from detoxification of H2O2 to redox signaling and differentiation. The relative stability of the selenoenzymes, however, remained enigmatic in view of the postulated involvement of a highly unstable selenenic acid form during catalysis. Nevertheless, density functional theory calculations obtained with a representative active site model verify the mechanistic concept of GPx catalysis and underscore its efficiency. However, they also allow that the selenenic acid, in the absence of the reducing substrate, reacts with a nitrogen in the active site. MS/MS analysis of oxidized rat GPx4 complies with the predicted structure, an 8-membered ring, in which selenium is bound as selenenylamide to the protein backbone. The intermediate can be re-integrated into the canonical GPx cycle by glutathione, whereas, under denaturing conditions, its selenium moiety undergoes β-cleavage with formation of a dehydro-alanine residue. The selenenylamide bypass prevents destruction of the redox center due to over-oxidation of the selenium or its elimination and likely allows fine-tuning of GPx activity or alternate substrate reactions for regulatory purposes. SecGPx Elsevier GPx1 Elsevier GPx4 Elsevier CysGPx(s) Elsevier CR Elsevier PC-OOH Elsevier NF-κB Elsevier 1-CysGPx(s) Elsevier MS1 Elsevier MS/MS Elsevier LC-ESI MS/MS Elsevier LC-MS/MS Elsevier DFT Elsevier CP Elsevier U Elsevier ESI Elsevier GSH Elsevier HPLC Elsevier CID Elsevier Q-TOF Elsevier MS Elsevier GPx(s) Elsevier GPx4U46C Elsevier RMSD Elsevier 2-CysGPx(s) Elsevier CS Elsevier RrGPx4 Elsevier Sec Elsevier LC-MS Elsevier Dha Elsevier TS Elsevier Mauri, Pierluigi oth Roveri, Antonella oth Toppo, Stefano oth Benazzi, Louise oth Bosello-Travain, Valentina oth De Palma, Antonella oth Maiorino, Matilde oth Miotto, Giovanni oth Zaccarin, Mattia oth Polimeno, Antonino oth Flohé, Leopold oth Ursini, Fulvio oth Enthalten in Elsevier Wu, Zhi-Sheng ELSEVIER New organic dyes with varied arylamine donors as effective co-sensitizers for ruthenium complex N719 in dye sensitized solar cells 2020 the official journal of the Oxygen Society, a constituent member of the International Society for Free Radical Research New York, NY [u.a.] (DE-627)ELV003689417 volume:87 year:2015 pages:1-14 extent:14 https://doi.org/10.1016/j.freeradbiomed.2015.06.011 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 52.57 Energiespeicherung VZ 53.36 Energiedirektumwandler elektrische Energiespeicher VZ AR 87 2015 1-14 14 045F 570 |
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New organic dyes with varied arylamine donors as effective co-sensitizers for ruthenium complex N719 in dye sensitized solar cells |
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Selenocysteine oxidation in glutathione peroxidase catalysis: an MS-supported quantum mechanics study |
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Selenocysteine oxidation in glutathione peroxidase catalysis: an MS-supported quantum mechanics study |
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Orian, Laura |
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New organic dyes with varied arylamine donors as effective co-sensitizers for ruthenium complex N719 in dye sensitized solar cells |
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New organic dyes with varied arylamine donors as effective co-sensitizers for ruthenium complex N719 in dye sensitized solar cells |
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selenocysteine oxidation in glutathione peroxidase catalysis: an ms-supported quantum mechanics study |
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Selenocysteine oxidation in glutathione peroxidase catalysis: an MS-supported quantum mechanics study |
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Glutathione peroxidases (GPxs) are enzymes working with either selenium or sulfur catalysis. They adopted diverse functions ranging from detoxification of H2O2 to redox signaling and differentiation. The relative stability of the selenoenzymes, however, remained enigmatic in view of the postulated involvement of a highly unstable selenenic acid form during catalysis. Nevertheless, density functional theory calculations obtained with a representative active site model verify the mechanistic concept of GPx catalysis and underscore its efficiency. However, they also allow that the selenenic acid, in the absence of the reducing substrate, reacts with a nitrogen in the active site. MS/MS analysis of oxidized rat GPx4 complies with the predicted structure, an 8-membered ring, in which selenium is bound as selenenylamide to the protein backbone. The intermediate can be re-integrated into the canonical GPx cycle by glutathione, whereas, under denaturing conditions, its selenium moiety undergoes β-cleavage with formation of a dehydro-alanine residue. The selenenylamide bypass prevents destruction of the redox center due to over-oxidation of the selenium or its elimination and likely allows fine-tuning of GPx activity or alternate substrate reactions for regulatory purposes. |
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Glutathione peroxidases (GPxs) are enzymes working with either selenium or sulfur catalysis. They adopted diverse functions ranging from detoxification of H2O2 to redox signaling and differentiation. The relative stability of the selenoenzymes, however, remained enigmatic in view of the postulated involvement of a highly unstable selenenic acid form during catalysis. Nevertheless, density functional theory calculations obtained with a representative active site model verify the mechanistic concept of GPx catalysis and underscore its efficiency. However, they also allow that the selenenic acid, in the absence of the reducing substrate, reacts with a nitrogen in the active site. MS/MS analysis of oxidized rat GPx4 complies with the predicted structure, an 8-membered ring, in which selenium is bound as selenenylamide to the protein backbone. The intermediate can be re-integrated into the canonical GPx cycle by glutathione, whereas, under denaturing conditions, its selenium moiety undergoes β-cleavage with formation of a dehydro-alanine residue. The selenenylamide bypass prevents destruction of the redox center due to over-oxidation of the selenium or its elimination and likely allows fine-tuning of GPx activity or alternate substrate reactions for regulatory purposes. |
| abstract_unstemmed |
Glutathione peroxidases (GPxs) are enzymes working with either selenium or sulfur catalysis. They adopted diverse functions ranging from detoxification of H2O2 to redox signaling and differentiation. The relative stability of the selenoenzymes, however, remained enigmatic in view of the postulated involvement of a highly unstable selenenic acid form during catalysis. Nevertheless, density functional theory calculations obtained with a representative active site model verify the mechanistic concept of GPx catalysis and underscore its efficiency. However, they also allow that the selenenic acid, in the absence of the reducing substrate, reacts with a nitrogen in the active site. MS/MS analysis of oxidized rat GPx4 complies with the predicted structure, an 8-membered ring, in which selenium is bound as selenenylamide to the protein backbone. The intermediate can be re-integrated into the canonical GPx cycle by glutathione, whereas, under denaturing conditions, its selenium moiety undergoes β-cleavage with formation of a dehydro-alanine residue. The selenenylamide bypass prevents destruction of the redox center due to over-oxidation of the selenium or its elimination and likely allows fine-tuning of GPx activity or alternate substrate reactions for regulatory purposes. |
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Selenocysteine oxidation in glutathione peroxidase catalysis: an MS-supported quantum mechanics study |
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Mauri, Pierluigi Roveri, Antonella Toppo, Stefano Benazzi, Louise Bosello-Travain, Valentina De Palma, Antonella Maiorino, Matilde Miotto, Giovanni Zaccarin, Mattia Polimeno, Antonino Flohé, Leopold Ursini, Fulvio |
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Mauri, Pierluigi Roveri, Antonella Toppo, Stefano Benazzi, Louise Bosello-Travain, Valentina De Palma, Antonella Maiorino, Matilde Miotto, Giovanni Zaccarin, Mattia Polimeno, Antonino Flohé, Leopold Ursini, Fulvio |
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