Bringing Nitric Oxide to the Molybdenum World

Detalhes bibliográficos
Autor(a) principal: Maia, Luísa
Data de Publicação: 2023
Tipo de documento: Outros
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10362/156748
Resumo: Molybdenum-containing enzymes of the xanthine oxidase (XO) family are well known to catalyse oxygen atom transfer reactions, with the great majority of the characterised enzymes catalysing the insertion of an oxygen atom into the substrate. Although some family members are known to catalyse the "reverse" reaction, the capability to abstract an oxygen atom from the substrate molecule is not generally recognised for these enzymes. Hence, it was with surprise and scepticism that the "molybdenum community" noticed the reports on the mammalian XO capability to catalyse the oxygen atom abstraction of nitrite to form nitric oxide (NO). The lack of precedent for a molybdenum- (or tungsten) containing nitrite reductase on the nitrogen biogeochemical cycle contributed also to the scepticism. It took several kinetic, spectroscopic and mechanistic studies on enzymes of the XO family and also of sulfite oxidase and DMSO reductase families to finally have wide recognition of the molybdoenzymes' ability to form NO from nitrite. Herein, integrated in a collection of "personal views" edited by Professor Ralf Mendel, is an overview of my personal journey on the XO and aldehyde oxidase-catalysed nitrite reduction to NO. The main research findings and the path followed to establish XO and AO as competent nitrite reductases are reviewed. The evidence suggesting that these enzymes are probable players of the mammalian NO metabolism is also discussed.
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spelling Bringing Nitric Oxide to the Molybdenum WorldA Personal Perspectivexanthine oxidasealdehyde oxidasemolybdenum enzymenitritehypoxianitric oxidecell signallingmoonlightingAnalytical ChemistryChemistry (miscellaneous)Molecular MedicineDrug DiscoveryPhysical and Theoretical ChemistryOrganic ChemistryMolybdenum-containing enzymes of the xanthine oxidase (XO) family are well known to catalyse oxygen atom transfer reactions, with the great majority of the characterised enzymes catalysing the insertion of an oxygen atom into the substrate. Although some family members are known to catalyse the "reverse" reaction, the capability to abstract an oxygen atom from the substrate molecule is not generally recognised for these enzymes. Hence, it was with surprise and scepticism that the "molybdenum community" noticed the reports on the mammalian XO capability to catalyse the oxygen atom abstraction of nitrite to form nitric oxide (NO). The lack of precedent for a molybdenum- (or tungsten) containing nitrite reductase on the nitrogen biogeochemical cycle contributed also to the scepticism. It took several kinetic, spectroscopic and mechanistic studies on enzymes of the XO family and also of sulfite oxidase and DMSO reductase families to finally have wide recognition of the molybdoenzymes' ability to form NO from nitrite. Herein, integrated in a collection of "personal views" edited by Professor Ralf Mendel, is an overview of my personal journey on the XO and aldehyde oxidase-catalysed nitrite reduction to NO. The main research findings and the path followed to establish XO and AO as competent nitrite reductases are reviewed. The evidence suggesting that these enzymes are probable players of the mammalian NO metabolism is also discussed.LAQV@REQUIMTEDQ - Departamento de QuímicaRUNMaia, Luísa2023-08-21T22:17:59Z2023-08-022023-08-02T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/other23application/pdfhttp://hdl.handle.net/10362/156748eng1420-3049PURE: 67973355https://doi.org/10.3390/molecules28155819info: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:RCAAP2024-05-22T18:13:43Zoai:run.unl.pt:10362/156748Portal AgregadorONGhttps://www.rcaap.pt/oai/openairemluisa.alvim@gmail.comopendoar:71602024-05-22T18:13:43Repositório 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 Bringing Nitric Oxide to the Molybdenum World
A Personal Perspective
title Bringing Nitric Oxide to the Molybdenum World
spellingShingle Bringing Nitric Oxide to the Molybdenum World
Maia, Luísa
xanthine oxidase
aldehyde oxidase
molybdenum enzyme
nitrite
hypoxia
nitric oxide
cell signalling
moonlighting
Analytical Chemistry
Chemistry (miscellaneous)
Molecular Medicine
Drug Discovery
Physical and Theoretical Chemistry
Organic Chemistry
title_short Bringing Nitric Oxide to the Molybdenum World
title_full Bringing Nitric Oxide to the Molybdenum World
title_fullStr Bringing Nitric Oxide to the Molybdenum World
title_full_unstemmed Bringing Nitric Oxide to the Molybdenum World
title_sort Bringing Nitric Oxide to the Molybdenum World
author Maia, Luísa
author_facet Maia, Luísa
author_role author
dc.contributor.none.fl_str_mv LAQV@REQUIMTE
DQ - Departamento de Química
RUN
dc.contributor.author.fl_str_mv Maia, Luísa
dc.subject.por.fl_str_mv xanthine oxidase
aldehyde oxidase
molybdenum enzyme
nitrite
hypoxia
nitric oxide
cell signalling
moonlighting
Analytical Chemistry
Chemistry (miscellaneous)
Molecular Medicine
Drug Discovery
Physical and Theoretical Chemistry
Organic Chemistry
topic xanthine oxidase
aldehyde oxidase
molybdenum enzyme
nitrite
hypoxia
nitric oxide
cell signalling
moonlighting
Analytical Chemistry
Chemistry (miscellaneous)
Molecular Medicine
Drug Discovery
Physical and Theoretical Chemistry
Organic Chemistry
description Molybdenum-containing enzymes of the xanthine oxidase (XO) family are well known to catalyse oxygen atom transfer reactions, with the great majority of the characterised enzymes catalysing the insertion of an oxygen atom into the substrate. Although some family members are known to catalyse the "reverse" reaction, the capability to abstract an oxygen atom from the substrate molecule is not generally recognised for these enzymes. Hence, it was with surprise and scepticism that the "molybdenum community" noticed the reports on the mammalian XO capability to catalyse the oxygen atom abstraction of nitrite to form nitric oxide (NO). The lack of precedent for a molybdenum- (or tungsten) containing nitrite reductase on the nitrogen biogeochemical cycle contributed also to the scepticism. It took several kinetic, spectroscopic and mechanistic studies on enzymes of the XO family and also of sulfite oxidase and DMSO reductase families to finally have wide recognition of the molybdoenzymes' ability to form NO from nitrite. Herein, integrated in a collection of "personal views" edited by Professor Ralf Mendel, is an overview of my personal journey on the XO and aldehyde oxidase-catalysed nitrite reduction to NO. The main research findings and the path followed to establish XO and AO as competent nitrite reductases are reviewed. The evidence suggesting that these enzymes are probable players of the mammalian NO metabolism is also discussed.
publishDate 2023
dc.date.none.fl_str_mv 2023-08-21T22:17:59Z
2023-08-02
2023-08-02T00:00:00Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
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status_str publishedVersion
dc.identifier.uri.fl_str_mv http://hdl.handle.net/10362/156748
url http://hdl.handle.net/10362/156748
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 1420-3049
PURE: 67973355
https://doi.org/10.3390/molecules28155819
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eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 23
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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