Putting xanthine oxidoreductase and aldehyde oxidase on the NO metabolism map: Nitrite reduction by molybdoenzymes
Nitric oxide radical (NO) is a signaling molecule involved in several physiological and pathological processes and a new nitrate-nitrite-NO pathway has emerged as a physiological alternative to the ''classic'' pathway of NO formation from L-arginine. Since the late 1990s, it has...
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Format: | Article |
Language: | English |
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Elsevier
2018-10-01
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Series: | Redox Biology |
Online Access: | http://www.sciencedirect.com/science/article/pii/S2213231718306657 |
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author | Luisa B. Maia José J.G. Moura |
author_facet | Luisa B. Maia José J.G. Moura |
author_sort | Luisa B. Maia |
collection | DOAJ |
description | Nitric oxide radical (NO) is a signaling molecule involved in several physiological and pathological processes and a new nitrate-nitrite-NO pathway has emerged as a physiological alternative to the ''classic'' pathway of NO formation from L-arginine. Since the late 1990s, it has become clear that nitrite can be reduced back to NO under hypoxic/anoxic conditions and exert a significant cytoprotective action in vivo under challenging conditions. To reduce nitrite to NO, mammalian cells can use different metalloproteins that are present in cells to perform other functions, including several heme proteins and molybdoenzymes, comprising what we denominated as the ''non-dedicated nitrite reductases''. Herein, we will review the current knowledge on two of those ''non-dedicated nitrite reductases'', the molybdoenzymes xanthine oxidoreductase and aldehyde oxidase, discussing the in vitro and in vivo studies to provide the current picture of the role of these enzymes on the NO metabolism in humans. Keywords: Nitric oxide, Nitrite, Xanthine oxidoreductase, Aldehyde oxidase, Oxygen availability, Molybdenum |
first_indexed | 2024-04-11T23:38:29Z |
format | Article |
id | doaj.art-e591a98edcce4730a53006f5673c5056 |
institution | Directory Open Access Journal |
issn | 2213-2317 |
language | English |
last_indexed | 2024-04-11T23:38:29Z |
publishDate | 2018-10-01 |
publisher | Elsevier |
record_format | Article |
series | Redox Biology |
spelling | doaj.art-e591a98edcce4730a53006f5673c50562022-12-22T03:56:52ZengElsevierRedox Biology2213-23172018-10-0119274289Putting xanthine oxidoreductase and aldehyde oxidase on the NO metabolism map: Nitrite reduction by molybdoenzymesLuisa B. Maia0José J.G. Moura1Corresponding author.; LAQV, REQUIMTE, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, 2829-516 Caparica, PortugalLAQV, REQUIMTE, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, 2829-516 Caparica, PortugalNitric oxide radical (NO) is a signaling molecule involved in several physiological and pathological processes and a new nitrate-nitrite-NO pathway has emerged as a physiological alternative to the ''classic'' pathway of NO formation from L-arginine. Since the late 1990s, it has become clear that nitrite can be reduced back to NO under hypoxic/anoxic conditions and exert a significant cytoprotective action in vivo under challenging conditions. To reduce nitrite to NO, mammalian cells can use different metalloproteins that are present in cells to perform other functions, including several heme proteins and molybdoenzymes, comprising what we denominated as the ''non-dedicated nitrite reductases''. Herein, we will review the current knowledge on two of those ''non-dedicated nitrite reductases'', the molybdoenzymes xanthine oxidoreductase and aldehyde oxidase, discussing the in vitro and in vivo studies to provide the current picture of the role of these enzymes on the NO metabolism in humans. Keywords: Nitric oxide, Nitrite, Xanthine oxidoreductase, Aldehyde oxidase, Oxygen availability, Molybdenumhttp://www.sciencedirect.com/science/article/pii/S2213231718306657 |
spellingShingle | Luisa B. Maia José J.G. Moura Putting xanthine oxidoreductase and aldehyde oxidase on the NO metabolism map: Nitrite reduction by molybdoenzymes Redox Biology |
title | Putting xanthine oxidoreductase and aldehyde oxidase on the NO metabolism map: Nitrite reduction by molybdoenzymes |
title_full | Putting xanthine oxidoreductase and aldehyde oxidase on the NO metabolism map: Nitrite reduction by molybdoenzymes |
title_fullStr | Putting xanthine oxidoreductase and aldehyde oxidase on the NO metabolism map: Nitrite reduction by molybdoenzymes |
title_full_unstemmed | Putting xanthine oxidoreductase and aldehyde oxidase on the NO metabolism map: Nitrite reduction by molybdoenzymes |
title_short | Putting xanthine oxidoreductase and aldehyde oxidase on the NO metabolism map: Nitrite reduction by molybdoenzymes |
title_sort | putting xanthine oxidoreductase and aldehyde oxidase on the no metabolism map nitrite reduction by molybdoenzymes |
url | http://www.sciencedirect.com/science/article/pii/S2213231718306657 |
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