Insights into determinants of the activity of the flavodiiron NO reductase from Escherichia coli

Detalhes bibliográficos
Autor(a) principal: Soares, Jéssica
Data de Publicação: 2020
Tipo de documento: Dissertação
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10362/112708
Resumo: "Flavodiiron proteins (FDPs) are a family of metalloproteins involved in the reduction of molecular oxygen and hydrogen peroxide to water and/or the reduction of nitric oxide to nitrous oxide. Bioinformatic analysis of the primary structure of the FDPs led to the identification of a conserved motif in class B FDPs (flavorubredoxins, FlRd), that is relatively close to the active centre. The present experimental work aimed to study the role played by two serines present in this motif in an FDP from E.coli. Thus, two mutants, S33D and S34D, were studied and characterized in order to determine the implications of such mutations on the biochemical, kinetic and spectroscopic properties of the enzyme. The production of the mutants was achieved in E. coli BL21 (DE3) Gold and it was found that the biochemical characteristics were kept almost unchanged.(...)"
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spelling Insights into determinants of the activity of the flavodiiron NO reductase from Escherichia coliFlavodiiron proteinsflavorubredoxinenzyme kinetic; electron paramagnetic resonanceBiochemistry for Health"Flavodiiron proteins (FDPs) are a family of metalloproteins involved in the reduction of molecular oxygen and hydrogen peroxide to water and/or the reduction of nitric oxide to nitrous oxide. Bioinformatic analysis of the primary structure of the FDPs led to the identification of a conserved motif in class B FDPs (flavorubredoxins, FlRd), that is relatively close to the active centre. The present experimental work aimed to study the role played by two serines present in this motif in an FDP from E.coli. Thus, two mutants, S33D and S34D, were studied and characterized in order to determine the implications of such mutations on the biochemical, kinetic and spectroscopic properties of the enzyme. The production of the mutants was achieved in E. coli BL21 (DE3) Gold and it was found that the biochemical characteristics were kept almost unchanged.(...)"Teixeira, MiguelRUNSoares, Jéssica2020-12-172020-122023-12-31T00:00:00Z2020-12-17T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/masterThesisapplication/pdfhttp://hdl.handle.net/10362/112708enginfo:eu-repo/semantics/embargoedAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2023-07-10T15:58:39ZPortal AgregadorONG
dc.title.none.fl_str_mv Insights into determinants of the activity of the flavodiiron NO reductase from Escherichia coli
title Insights into determinants of the activity of the flavodiiron NO reductase from Escherichia coli
spellingShingle Insights into determinants of the activity of the flavodiiron NO reductase from Escherichia coli
Soares, Jéssica
Flavodiiron proteins
flavorubredoxin
enzyme kinetic
; electron paramagnetic resonance
Biochemistry for Health
title_short Insights into determinants of the activity of the flavodiiron NO reductase from Escherichia coli
title_full Insights into determinants of the activity of the flavodiiron NO reductase from Escherichia coli
title_fullStr Insights into determinants of the activity of the flavodiiron NO reductase from Escherichia coli
title_full_unstemmed Insights into determinants of the activity of the flavodiiron NO reductase from Escherichia coli
title_sort Insights into determinants of the activity of the flavodiiron NO reductase from Escherichia coli
author Soares, Jéssica
author_facet Soares, Jéssica
author_role author
dc.contributor.none.fl_str_mv Teixeira, Miguel
RUN
dc.contributor.author.fl_str_mv Soares, Jéssica
dc.subject.por.fl_str_mv Flavodiiron proteins
flavorubredoxin
enzyme kinetic
; electron paramagnetic resonance
Biochemistry for Health
topic Flavodiiron proteins
flavorubredoxin
enzyme kinetic
; electron paramagnetic resonance
Biochemistry for Health
description "Flavodiiron proteins (FDPs) are a family of metalloproteins involved in the reduction of molecular oxygen and hydrogen peroxide to water and/or the reduction of nitric oxide to nitrous oxide. Bioinformatic analysis of the primary structure of the FDPs led to the identification of a conserved motif in class B FDPs (flavorubredoxins, FlRd), that is relatively close to the active centre. The present experimental work aimed to study the role played by two serines present in this motif in an FDP from E.coli. Thus, two mutants, S33D and S34D, were studied and characterized in order to determine the implications of such mutations on the biochemical, kinetic and spectroscopic properties of the enzyme. The production of the mutants was achieved in E. coli BL21 (DE3) Gold and it was found that the biochemical characteristics were kept almost unchanged.(...)"
publishDate 2020
dc.date.none.fl_str_mv 2020-12-17
2020-12
2020-12-17T00:00:00Z
2023-12-31T00:00:00Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/masterThesis
format masterThesis
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://hdl.handle.net/10362/112708
url http://hdl.handle.net/10362/112708
dc.language.iso.fl_str_mv eng
language eng
dc.rights.driver.fl_str_mv info:eu-repo/semantics/embargoedAccess
eu_rights_str_mv embargoedAccess
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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instacron_str RCAAP
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collection Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
repository.name.fl_str_mv
repository.mail.fl_str_mv
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