Steady-state kinetics with nitric oxide reductase (NOR)

Detalhes bibliográficos
Autor(a) principal: Duarte, Américo G.
Data de Publicação: 2014
Outros Autores: Cordas, Cristina, Moura, José João Galhardas de, Moura, Isabel Maria Andrade Martins Galhardas de
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10362/36567
Resumo: We would like to thank Fundacao para a Ciencia e Tecnologia for the financial support through grants SFRH/BD/39009/2007 (AGD), PDTC/QUI/64638/2006 (IM) and PDCT/QUI-BIOQ/1/6481/2010 (IM). REQUIMTE is funded by grant PEst-C/EQB/LA0006/2013 from FCT/MEC.
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spelling Steady-state kinetics with nitric oxide reductase (NOR)new considerations on substrate inhibition profile and catalytic mechanismElectrochemistryEnzyme kineticsNO reductionNORWe would like to thank Fundacao para a Ciencia e Tecnologia for the financial support through grants SFRH/BD/39009/2007 (AGD), PDTC/QUI/64638/2006 (IM) and PDCT/QUI-BIOQ/1/6481/2010 (IM). REQUIMTE is funded by grant PEst-C/EQB/LA0006/2013 from FCT/MEC.Nitric oxide reductase (NOR) from denitrifying bacteria is an integral membrane protein that catalyses the two electron reduction of NO to N2O, as part of the denitrification process, being responsible for an exclusive reaction, the NN bond formation, the key step of this metabolic pathway. Additionally, this class of enzymes also presents residual oxidoreductase activity, reducing O2 to H2O in a four electron/proton reaction. In this work we report, for the first time, steady-state kinetics with the Pseudomonas nautica NOR, either in the presence of its physiological electron donor (cyt. c552) or immobilised on a graphite electrode surface, in the presence of its known substrates, namely NO or O2. The obtained results show that the enzyme has high affinity for its natural substrate, NO, and different kinetic profiles according to the electron donor used. The kinetic data, as shown by the pH dependence, is modelled by ionisable amino acid residues nearby the di-nuclear catalytic site. The catalytic mechanism is revised and a mononitrosyl-non-heme Fe complex (FeB(II)-NO) species is favoured as the first catalytic intermediate involved on the NO reduction.Instituto de Tecnologia Química e Biológica António Xavier (ITQB)DQ - Departamento de QuímicaCQFB-REQUIMTE - Centro de Química Fina e Biotecnologia (Lab. Associado REQUIMTE)RUNDuarte, Américo G.Cordas, CristinaMoura, José João Galhardas deMoura, Isabel Maria Andrade Martins Galhardas de2018-05-11T22:01:17Z2014-032014-03-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10362/36567eng0005-2728PURE: 379702https://doi.org/10.1016/j.bbabio.2014.01.001info: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:RCAAP2024-03-11T04:20:01Zoai:run.unl.pt:10362/36567Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T03:30:33.791833Repositório 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 Steady-state kinetics with nitric oxide reductase (NOR)
new considerations on substrate inhibition profile and catalytic mechanism
title Steady-state kinetics with nitric oxide reductase (NOR)
spellingShingle Steady-state kinetics with nitric oxide reductase (NOR)
Duarte, Américo G.
Electrochemistry
Enzyme kinetics
NO reduction
NOR
title_short Steady-state kinetics with nitric oxide reductase (NOR)
title_full Steady-state kinetics with nitric oxide reductase (NOR)
title_fullStr Steady-state kinetics with nitric oxide reductase (NOR)
title_full_unstemmed Steady-state kinetics with nitric oxide reductase (NOR)
title_sort Steady-state kinetics with nitric oxide reductase (NOR)
author Duarte, Américo G.
author_facet Duarte, Américo G.
Cordas, Cristina
Moura, José João Galhardas de
Moura, Isabel Maria Andrade Martins Galhardas de
author_role author
author2 Cordas, Cristina
Moura, José João Galhardas de
Moura, Isabel Maria Andrade Martins Galhardas de
author2_role author
author
author
dc.contributor.none.fl_str_mv Instituto de Tecnologia Química e Biológica António Xavier (ITQB)
DQ - Departamento de Química
CQFB-REQUIMTE - Centro de Química Fina e Biotecnologia (Lab. Associado REQUIMTE)
RUN
dc.contributor.author.fl_str_mv Duarte, Américo G.
Cordas, Cristina
Moura, José João Galhardas de
Moura, Isabel Maria Andrade Martins Galhardas de
dc.subject.por.fl_str_mv Electrochemistry
Enzyme kinetics
NO reduction
NOR
topic Electrochemistry
Enzyme kinetics
NO reduction
NOR
description We would like to thank Fundacao para a Ciencia e Tecnologia for the financial support through grants SFRH/BD/39009/2007 (AGD), PDTC/QUI/64638/2006 (IM) and PDCT/QUI-BIOQ/1/6481/2010 (IM). REQUIMTE is funded by grant PEst-C/EQB/LA0006/2013 from FCT/MEC.
publishDate 2014
dc.date.none.fl_str_mv 2014-03
2014-03-01T00:00:00Z
2018-05-11T22:01:17Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://hdl.handle.net/10362/36567
url http://hdl.handle.net/10362/36567
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 0005-2728
PURE: 379702
https://doi.org/10.1016/j.bbabio.2014.01.001
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
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