Steady-state kinetics with nitric oxide reductase (NOR)
Autor(a) principal: | |
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Data de Publicação: | 2014 |
Outros Autores: | , , |
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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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 |
dc.format.none.fl_str_mv |
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 |
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Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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RCAAP |
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RCAAP |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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1799137929798352896 |