Putting xanthine oxidoreductase and aldehyde oxidase on the NO metabolism map: Nitrite reduction by molybdoenzymes

Detalhes bibliográficos
Autor(a) principal: Maia, Luisa B.
Data de Publicação: 2018
Outros Autores: Moura, José J.G.
Tipo de documento: Outros
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: https://doi.org/10.1016/j.redox.2018.08.020
Resumo: We acknowledge Fundacao para a Ciencia e Tecnologia (FCT/MCTES) for the financial support granted to the Associate Laboratory for Green Chemistry - LAQV, which is financed by national funds from FCT/MCTES (UID/QUI/50006/2013) and co-financed by the ERDF under the PT2020 Partnership Agreement (POCI-01-0145-FEDER - 007265). LBM also thanks to FCT/MCTES for the fellowship grant (SFRH/BPD/111404/2015, which is financed by national funds and co-financed by FSE).
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spelling Putting xanthine oxidoreductase and aldehyde oxidase on the NO metabolism map: Nitrite reduction by molybdoenzymesAldehyde oxidaseMolybdenumNitric oxideNitriteOxygen availabilityXanthine oxidoreductaseOrganic ChemistryClinical BiochemistryWe acknowledge Fundacao para a Ciencia e Tecnologia (FCT/MCTES) for the financial support granted to the Associate Laboratory for Green Chemistry - LAQV, which is financed by national funds from FCT/MCTES (UID/QUI/50006/2013) and co-financed by the ERDF under the PT2020 Partnership Agreement (POCI-01-0145-FEDER - 007265). LBM also thanks to FCT/MCTES for the fellowship grant (SFRH/BPD/111404/2015, which is financed by national funds and co-financed by FSE).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.LAQV@REQUIMTEDQ - Departamento de QuímicaRUNMaia, Luisa B.Moura, José J.G.2019-01-28T23:30:12Z2018-10-012018-10-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/other16application/pdfhttps://doi.org/10.1016/j.redox.2018.08.020eng2213-2317PURE: 5882201http://www.scopus.com/inward/record.url?scp=85052926683&partnerID=8YFLogxKhttps://doi.org/10.1016/j.redox.2018.08.020info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2024-05-22T17:36:51Zoai:run.unl.pt:10362/58902Portal AgregadorONGhttps://www.rcaap.pt/oai/openairemluisa.alvim@gmail.comopendoar:71602024-05-22T17:36:51Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse
dc.title.none.fl_str_mv Putting xanthine oxidoreductase and aldehyde oxidase on the NO metabolism map: Nitrite reduction by molybdoenzymes
title Putting xanthine oxidoreductase and aldehyde oxidase on the NO metabolism map: Nitrite reduction by molybdoenzymes
spellingShingle Putting xanthine oxidoreductase and aldehyde oxidase on the NO metabolism map: Nitrite reduction by molybdoenzymes
Maia, Luisa B.
Aldehyde oxidase
Molybdenum
Nitric oxide
Nitrite
Oxygen availability
Xanthine oxidoreductase
Organic Chemistry
Clinical Biochemistry
title_short 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_sort Putting xanthine oxidoreductase and aldehyde oxidase on the NO metabolism map: Nitrite reduction by molybdoenzymes
author Maia, Luisa B.
author_facet Maia, Luisa B.
Moura, José J.G.
author_role author
author2 Moura, José J.G.
author2_role author
dc.contributor.none.fl_str_mv LAQV@REQUIMTE
DQ - Departamento de Química
RUN
dc.contributor.author.fl_str_mv Maia, Luisa B.
Moura, José J.G.
dc.subject.por.fl_str_mv Aldehyde oxidase
Molybdenum
Nitric oxide
Nitrite
Oxygen availability
Xanthine oxidoreductase
Organic Chemistry
Clinical Biochemistry
topic Aldehyde oxidase
Molybdenum
Nitric oxide
Nitrite
Oxygen availability
Xanthine oxidoreductase
Organic Chemistry
Clinical Biochemistry
description We acknowledge Fundacao para a Ciencia e Tecnologia (FCT/MCTES) for the financial support granted to the Associate Laboratory for Green Chemistry - LAQV, which is financed by national funds from FCT/MCTES (UID/QUI/50006/2013) and co-financed by the ERDF under the PT2020 Partnership Agreement (POCI-01-0145-FEDER - 007265). LBM also thanks to FCT/MCTES for the fellowship grant (SFRH/BPD/111404/2015, which is financed by national funds and co-financed by FSE).
publishDate 2018
dc.date.none.fl_str_mv 2018-10-01
2018-10-01T00:00:00Z
2019-01-28T23:30:12Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/other
format other
status_str publishedVersion
dc.identifier.uri.fl_str_mv https://doi.org/10.1016/j.redox.2018.08.020
url https://doi.org/10.1016/j.redox.2018.08.020
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 2213-2317
PURE: 5882201
http://www.scopus.com/inward/record.url?scp=85052926683&partnerID=8YFLogxK
https://doi.org/10.1016/j.redox.2018.08.020
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 16
application/pdf
dc.source.none.fl_str_mv reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron:RCAAP
instname_str Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron_str RCAAP
institution RCAAP
reponame_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
collection Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
repository.name.fl_str_mv Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
repository.mail.fl_str_mv mluisa.alvim@gmail.com
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