Xanthine oxidase converts nitric oxide to nitroxyl that inactivates the enzyme
Xanthine oxidase (XO) was found to convert nitric oxide (NO* ) released from spermine-NONOate to nitroxyl (HNO), the one-electron reduction product of NO*, in the presence of its substrate hypoxanthine under anaerobic conditions. Under these conditions, XO lost its activity. Upon aerobic incubation of XO with its substrate, neither conversion of NO* to HNO nor inactivation of the enzyme was observed. Angeli's salt (an HNO generator) or synthetic peroxynitrite inactivated XO at low concentrations, whereas high concentrations of diethylamine-NONOate (an NO* donor) and SIN-1 (which generates peroxynitrite by releasing both NO* and superoxide) were required to inactivate XO. These results suggest that HNO generated by XO under anaerobic conditions inactivates XO. As both XO and NO* synthase are activated and/or induced in ischemia-reperfusion injury, HNO formed by XO may contribute to pathogenesis by exerting its potent oxidation activity against a variety of biological compounds.
| Medienart: |
Artikel |
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| Erscheinungsjahr: |
2004 |
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| Erschienen: |
2004 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:315 |
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| Enthalten in: |
Biochemical and biophysical research communications - 315(2004), 2 vom: 05. März, Seite 455-62 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Saleem, Mohammad [VerfasserIn] |
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| Anmerkungen: |
Date Completed 20.04.2004 Date Revised 24.11.2016 published: Print Citation Status MEDLINE |
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| Förderinstitution / Projekttitel: |
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| PPN (Katalog-ID): |
NLM144706490 |
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| 100 | 1 | |a Saleem, Mohammad |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a Xanthine oxidase converts nitric oxide to nitroxyl that inactivates the enzyme |
| 264 | 1 | |c 2004 | |
| 336 | |a Text |b txt |2 rdacontent | ||
| 337 | |a ohne Hilfsmittel zu benutzen |b n |2 rdamedia | ||
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| 500 | |a Date Completed 20.04.2004 | ||
| 500 | |a Date Revised 24.11.2016 | ||
| 500 | |a published: Print | ||
| 500 | |a Citation Status MEDLINE | ||
| 520 | |a Xanthine oxidase (XO) was found to convert nitric oxide (NO* ) released from spermine-NONOate to nitroxyl (HNO), the one-electron reduction product of NO*, in the presence of its substrate hypoxanthine under anaerobic conditions. Under these conditions, XO lost its activity. Upon aerobic incubation of XO with its substrate, neither conversion of NO* to HNO nor inactivation of the enzyme was observed. Angeli's salt (an HNO generator) or synthetic peroxynitrite inactivated XO at low concentrations, whereas high concentrations of diethylamine-NONOate (an NO* donor) and SIN-1 (which generates peroxynitrite by releasing both NO* and superoxide) were required to inactivate XO. These results suggest that HNO generated by XO under anaerobic conditions inactivates XO. As both XO and NO* synthase are activated and/or induced in ischemia-reperfusion injury, HNO formed by XO may contribute to pathogenesis by exerting its potent oxidation activity against a variety of biological compounds | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Research Support, Non-U.S. Gov't | |
| 650 | 7 | |a Hemoglobins |2 NLM | |
| 650 | 7 | |a Nitrites |2 NLM | |
| 650 | 7 | |a Nitrogen Oxides |2 NLM | |
| 650 | 7 | |a Reactive Nitrogen Species |2 NLM | |
| 650 | 7 | |a nitrosyl hemoglobin |2 NLM | |
| 650 | 7 | |a Peroxynitrous Acid |2 NLM | |
| 650 | 7 | |a 14691-52-2 |2 NLM | |
| 650 | 7 | |a Xanthine |2 NLM | |
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| 650 | 7 | |a Spermine |2 NLM | |
| 650 | 7 | |a 2FZ7Y3VOQX |2 NLM | |
| 650 | 7 | |a Nitric Oxide |2 NLM | |
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| 650 | 7 | |a linsidomine |2 NLM | |
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| 650 | 7 | |a Molsidomine |2 NLM | |
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| 650 | 7 | |a Xanthine Oxidase |2 NLM | |
| 650 | 7 | |a EC 1.17.3.2 |2 NLM | |
| 650 | 7 | |a nitroxyl |2 NLM | |
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| 650 | 7 | |a Oxygen |2 NLM | |
| 650 | 7 | |a S88TT14065 |2 NLM | |
| 700 | 1 | |a Ohshima, Hiroshi |e verfasserin |4 aut | |
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