Biochemical and biophysical characterization of a truncated NADH dehydrogenase-2 of Escherichia coli

Autores
Villegas, Josefina Maria; Torres Bugeau, Clarisa Maria; Burgos, Martha Ines; Fidelio, Gerardo Daniel; Chehin, Rosana Nieves; Rintoul, Maria Regina; Rapisarda, Viviana Andrea
Año de publicación
2012
Idioma
inglés
Tipo de recurso
documento de conferencia
Estado
versión publicada
Descripción
NADH dehydrogenase-2 (NDH-2) of Escherichia coli is a flavoprotein bound to the membrane by its C-terminal region. We have constructed a water soluble protein, Trun-3, eliminating the last 43 aminoacids of NDH-2. Despite FAD cofactor was absent in the purified truncated protein, its enzymatic activity was reconstituted by the addition of 10 ìM FAD. Here, far-UV circular dichroism (CD), Fourier transform infrared (FTIR) spectroscopy, fluorescence spectroscopy and limited proteolysis experiments provided evidence for a FAD-induced conformational change in Trun-3. For instance, a significant decrease in intrinsic fluorescence emission took place upon FAD binding, which could be related to conformational rearrangements that would affect the local environment of the protein tryptophan residues. Also, the limited digestion experiment with trypsin revealed a different fragmentation pattern in the presence of FAD compared to that of the apo-Trun-3, indicating that FAD binding has an effect on the protein conformation. However, CD data indicated that secondary structure of the apoprotein was hardly affected by the binding of the flavin since Trun-3 had the same structural component ratios independently of its cofactor. Similar results were observed by FTIR. Apparent melting temperatures and thermal inactivation kinetics showed that cofactor binding to apoenzyme lead to a slight thermal stabilization of holoenzyme. Taking together, FAD binding affects tertiary structure, while slightly changes the secondary structure of Trun-3. A broad knowledge about NDH-2s could promote their potential applications in medical science, as chemotherapeutic targets or in gene therapy.Escherichia coli is a flavoprotein bound to the membrane by its C-terminal region. We have constructed a water soluble protein, Trun-3, eliminating the last 43 aminoacids of NDH-2. Despite FAD cofactor was absent in the purified truncated protein, its enzymatic activity was reconstituted by the addition of 10 ìM FAD. Here, far-UV circular dichroism (CD), Fourier transform infrared (FTIR) spectroscopy, fluorescence spectroscopy and limited proteolysis experiments provided evidence for a FAD-induced conformational change in Trun-3. For instance, a significant decrease in intrinsic fluorescence emission took place upon FAD binding, which could be related to conformational rearrangements that would affect the local environment of the protein tryptophan residues. Also, the limited digestion experiment with trypsin revealed a different fragmentation pattern in the presence of FAD compared to that of the apo-Trun-3, indicating that FAD binding has an effect on the protein conformation. However, CD data indicated that secondary structure of the apoprotein was hardly affected by the binding of the flavin since Trun-3 had the same structural component ratios independently of its cofactor. Similar results were observed by FTIR. Apparent melting temperatures and thermal inactivation kinetics showed that cofactor binding to apoenzyme lead to a slight thermal stabilization of holoenzyme. Taking together, FAD binding affects tertiary structure, while slightly changes the secondary structure of Trun-3. A broad knowledge about NDH-2s could promote their potential applications in medical science, as chemotherapeutic targets or in gene therapy.
Fil: Villegas, Josefina Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
Fil: Torres Bugeau, Clarisa Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
Fil: Burgos, Martha Ines. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
Fil: Fidelio, Gerardo Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
Fil: Chehin, Rosana Nieves. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
Fil: Rintoul, Maria Regina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
Fil: Rapisarda, Viviana Andrea. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
XLI Reunião Anual da Sociedade Brasileira de Bioquímica e Biologia Molecular
Foz do Iguacu
Brasil
Sociedade Brasileira de Bioquímica e Biologia Molecular
Materia
FAD
NADH
ESCHERICHIA COLI
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
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Consejo Nacional de Investigaciones Científicas y Técnicas
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oai:ri.conicet.gov.ar:11336/235545
Acceder
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network_name_str CONICET Digital (CONICET)
spelling Biochemical and biophysical characterization of a truncated NADH dehydrogenase-2 of Escherichia coliVillegas, Josefina MariaTorres Bugeau, Clarisa MariaBurgos, Martha InesFidelio, Gerardo DanielChehin, Rosana NievesRintoul, Maria ReginaRapisarda, Viviana AndreaFADNADHESCHERICHIA COLIhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1NADH dehydrogenase-2 (NDH-2) of Escherichia coli is a flavoprotein bound to the membrane by its C-terminal region. We have constructed a water soluble protein, Trun-3, eliminating the last 43 aminoacids of NDH-2. Despite FAD cofactor was absent in the purified truncated protein, its enzymatic activity was reconstituted by the addition of 10 ìM FAD. Here, far-UV circular dichroism (CD), Fourier transform infrared (FTIR) spectroscopy, fluorescence spectroscopy and limited proteolysis experiments provided evidence for a FAD-induced conformational change in Trun-3. For instance, a significant decrease in intrinsic fluorescence emission took place upon FAD binding, which could be related to conformational rearrangements that would affect the local environment of the protein tryptophan residues. Also, the limited digestion experiment with trypsin revealed a different fragmentation pattern in the presence of FAD compared to that of the apo-Trun-3, indicating that FAD binding has an effect on the protein conformation. However, CD data indicated that secondary structure of the apoprotein was hardly affected by the binding of the flavin since Trun-3 had the same structural component ratios independently of its cofactor. Similar results were observed by FTIR. Apparent melting temperatures and thermal inactivation kinetics showed that cofactor binding to apoenzyme lead to a slight thermal stabilization of holoenzyme. Taking together, FAD binding affects tertiary structure, while slightly changes the secondary structure of Trun-3. A broad knowledge about NDH-2s could promote their potential applications in medical science, as chemotherapeutic targets or in gene therapy.Escherichia coli is a flavoprotein bound to the membrane by its C-terminal region. We have constructed a water soluble protein, Trun-3, eliminating the last 43 aminoacids of NDH-2. Despite FAD cofactor was absent in the purified truncated protein, its enzymatic activity was reconstituted by the addition of 10 ìM FAD. Here, far-UV circular dichroism (CD), Fourier transform infrared (FTIR) spectroscopy, fluorescence spectroscopy and limited proteolysis experiments provided evidence for a FAD-induced conformational change in Trun-3. For instance, a significant decrease in intrinsic fluorescence emission took place upon FAD binding, which could be related to conformational rearrangements that would affect the local environment of the protein tryptophan residues. Also, the limited digestion experiment with trypsin revealed a different fragmentation pattern in the presence of FAD compared to that of the apo-Trun-3, indicating that FAD binding has an effect on the protein conformation. However, CD data indicated that secondary structure of the apoprotein was hardly affected by the binding of the flavin since Trun-3 had the same structural component ratios independently of its cofactor. Similar results were observed by FTIR. Apparent melting temperatures and thermal inactivation kinetics showed that cofactor binding to apoenzyme lead to a slight thermal stabilization of holoenzyme. Taking together, FAD binding affects tertiary structure, while slightly changes the secondary structure of Trun-3. A broad knowledge about NDH-2s could promote their potential applications in medical science, as chemotherapeutic targets or in gene therapy.Fil: Villegas, Josefina Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; ArgentinaFil: Torres Bugeau, Clarisa Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; ArgentinaFil: Burgos, Martha Ines. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; ArgentinaFil: Fidelio, Gerardo Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; ArgentinaFil: Chehin, Rosana Nieves. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; ArgentinaFil: Rintoul, Maria Regina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; ArgentinaFil: Rapisarda, Viviana Andrea. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; ArgentinaXLI Reunião Anual da Sociedade Brasileira de Bioquímica e Biologia MolecularFoz do IguacuBrasilSociedade Brasileira de Bioquímica e Biologia MolecularSociedade Brasileira de Bioquímica e Biologia Molecular2012info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/conferenceObjectReuniónBookhttp://purl.org/coar/resource_type/c_5794info:ar-repo/semantics/documentoDeConferenciaapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/235545Biochemical and biophysical characterization of a truncated NADH dehydrogenase-2 of Escherichia coli; XLI Reunião Anual da Sociedade Brasileira de Bioquímica e Biologia Molecular; Foz do Iguacu; Brasil; 2012; 1-1CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www2.sbbq.org.br/reuniao/cdrom/ra2012/resumos/R9191.pdfInternacionalinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T11:34:45Zoai:ri.conicet.gov.ar:11336/235545instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-10-22 11:34:46.15CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Biochemical and biophysical characterization of a truncated NADH dehydrogenase-2 of Escherichia coli
title Biochemical and biophysical characterization of a truncated NADH dehydrogenase-2 of Escherichia coli
spellingShingle Biochemical and biophysical characterization of a truncated NADH dehydrogenase-2 of Escherichia coli
Villegas, Josefina Maria
FAD
NADH
ESCHERICHIA COLI
title_short Biochemical and biophysical characterization of a truncated NADH dehydrogenase-2 of Escherichia coli
title_full Biochemical and biophysical characterization of a truncated NADH dehydrogenase-2 of Escherichia coli
title_fullStr Biochemical and biophysical characterization of a truncated NADH dehydrogenase-2 of Escherichia coli
title_full_unstemmed Biochemical and biophysical characterization of a truncated NADH dehydrogenase-2 of Escherichia coli
title_sort Biochemical and biophysical characterization of a truncated NADH dehydrogenase-2 of Escherichia coli
dc.creator.none.fl_str_mv Villegas, Josefina Maria
Torres Bugeau, Clarisa Maria
Burgos, Martha Ines
Fidelio, Gerardo Daniel
Chehin, Rosana Nieves
Rintoul, Maria Regina
Rapisarda, Viviana Andrea
author Villegas, Josefina Maria
author_facet Villegas, Josefina Maria
Torres Bugeau, Clarisa Maria
Burgos, Martha Ines
Fidelio, Gerardo Daniel
Chehin, Rosana Nieves
Rintoul, Maria Regina
Rapisarda, Viviana Andrea
author_role author
author2 Torres Bugeau, Clarisa Maria
Burgos, Martha Ines
Fidelio, Gerardo Daniel
Chehin, Rosana Nieves
Rintoul, Maria Regina
Rapisarda, Viviana Andrea
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv FAD
NADH
ESCHERICHIA COLI
topic FAD
NADH
ESCHERICHIA COLI
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv NADH dehydrogenase-2 (NDH-2) of Escherichia coli is a flavoprotein bound to the membrane by its C-terminal region. We have constructed a water soluble protein, Trun-3, eliminating the last 43 aminoacids of NDH-2. Despite FAD cofactor was absent in the purified truncated protein, its enzymatic activity was reconstituted by the addition of 10 ìM FAD. Here, far-UV circular dichroism (CD), Fourier transform infrared (FTIR) spectroscopy, fluorescence spectroscopy and limited proteolysis experiments provided evidence for a FAD-induced conformational change in Trun-3. For instance, a significant decrease in intrinsic fluorescence emission took place upon FAD binding, which could be related to conformational rearrangements that would affect the local environment of the protein tryptophan residues. Also, the limited digestion experiment with trypsin revealed a different fragmentation pattern in the presence of FAD compared to that of the apo-Trun-3, indicating that FAD binding has an effect on the protein conformation. However, CD data indicated that secondary structure of the apoprotein was hardly affected by the binding of the flavin since Trun-3 had the same structural component ratios independently of its cofactor. Similar results were observed by FTIR. Apparent melting temperatures and thermal inactivation kinetics showed that cofactor binding to apoenzyme lead to a slight thermal stabilization of holoenzyme. Taking together, FAD binding affects tertiary structure, while slightly changes the secondary structure of Trun-3. A broad knowledge about NDH-2s could promote their potential applications in medical science, as chemotherapeutic targets or in gene therapy.Escherichia coli is a flavoprotein bound to the membrane by its C-terminal region. We have constructed a water soluble protein, Trun-3, eliminating the last 43 aminoacids of NDH-2. Despite FAD cofactor was absent in the purified truncated protein, its enzymatic activity was reconstituted by the addition of 10 ìM FAD. Here, far-UV circular dichroism (CD), Fourier transform infrared (FTIR) spectroscopy, fluorescence spectroscopy and limited proteolysis experiments provided evidence for a FAD-induced conformational change in Trun-3. For instance, a significant decrease in intrinsic fluorescence emission took place upon FAD binding, which could be related to conformational rearrangements that would affect the local environment of the protein tryptophan residues. Also, the limited digestion experiment with trypsin revealed a different fragmentation pattern in the presence of FAD compared to that of the apo-Trun-3, indicating that FAD binding has an effect on the protein conformation. However, CD data indicated that secondary structure of the apoprotein was hardly affected by the binding of the flavin since Trun-3 had the same structural component ratios independently of its cofactor. Similar results were observed by FTIR. Apparent melting temperatures and thermal inactivation kinetics showed that cofactor binding to apoenzyme lead to a slight thermal stabilization of holoenzyme. Taking together, FAD binding affects tertiary structure, while slightly changes the secondary structure of Trun-3. A broad knowledge about NDH-2s could promote their potential applications in medical science, as chemotherapeutic targets or in gene therapy.
Fil: Villegas, Josefina Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
Fil: Torres Bugeau, Clarisa Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
Fil: Burgos, Martha Ines. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
Fil: Fidelio, Gerardo Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
Fil: Chehin, Rosana Nieves. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
Fil: Rintoul, Maria Regina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
Fil: Rapisarda, Viviana Andrea. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
XLI Reunião Anual da Sociedade Brasileira de Bioquímica e Biologia Molecular
Foz do Iguacu
Brasil
Sociedade Brasileira de Bioquímica e Biologia Molecular
description NADH dehydrogenase-2 (NDH-2) of Escherichia coli is a flavoprotein bound to the membrane by its C-terminal region. We have constructed a water soluble protein, Trun-3, eliminating the last 43 aminoacids of NDH-2. Despite FAD cofactor was absent in the purified truncated protein, its enzymatic activity was reconstituted by the addition of 10 ìM FAD. Here, far-UV circular dichroism (CD), Fourier transform infrared (FTIR) spectroscopy, fluorescence spectroscopy and limited proteolysis experiments provided evidence for a FAD-induced conformational change in Trun-3. For instance, a significant decrease in intrinsic fluorescence emission took place upon FAD binding, which could be related to conformational rearrangements that would affect the local environment of the protein tryptophan residues. Also, the limited digestion experiment with trypsin revealed a different fragmentation pattern in the presence of FAD compared to that of the apo-Trun-3, indicating that FAD binding has an effect on the protein conformation. However, CD data indicated that secondary structure of the apoprotein was hardly affected by the binding of the flavin since Trun-3 had the same structural component ratios independently of its cofactor. Similar results were observed by FTIR. Apparent melting temperatures and thermal inactivation kinetics showed that cofactor binding to apoenzyme lead to a slight thermal stabilization of holoenzyme. Taking together, FAD binding affects tertiary structure, while slightly changes the secondary structure of Trun-3. A broad knowledge about NDH-2s could promote their potential applications in medical science, as chemotherapeutic targets or in gene therapy.Escherichia coli is a flavoprotein bound to the membrane by its C-terminal region. We have constructed a water soluble protein, Trun-3, eliminating the last 43 aminoacids of NDH-2. Despite FAD cofactor was absent in the purified truncated protein, its enzymatic activity was reconstituted by the addition of 10 ìM FAD. Here, far-UV circular dichroism (CD), Fourier transform infrared (FTIR) spectroscopy, fluorescence spectroscopy and limited proteolysis experiments provided evidence for a FAD-induced conformational change in Trun-3. For instance, a significant decrease in intrinsic fluorescence emission took place upon FAD binding, which could be related to conformational rearrangements that would affect the local environment of the protein tryptophan residues. Also, the limited digestion experiment with trypsin revealed a different fragmentation pattern in the presence of FAD compared to that of the apo-Trun-3, indicating that FAD binding has an effect on the protein conformation. However, CD data indicated that secondary structure of the apoprotein was hardly affected by the binding of the flavin since Trun-3 had the same structural component ratios independently of its cofactor. Similar results were observed by FTIR. Apparent melting temperatures and thermal inactivation kinetics showed that cofactor binding to apoenzyme lead to a slight thermal stabilization of holoenzyme. Taking together, FAD binding affects tertiary structure, while slightly changes the secondary structure of Trun-3. A broad knowledge about NDH-2s could promote their potential applications in medical science, as chemotherapeutic targets or in gene therapy.
publishDate 2012
dc.date.none.fl_str_mv 2012
dc.type.none.fl_str_mv info:eu-repo/semantics/publishedVersion
info:eu-repo/semantics/conferenceObject
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Book
http://purl.org/coar/resource_type/c_5794
info:ar-repo/semantics/documentoDeConferencia
status_str publishedVersion
format conferenceObject
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/235545
Biochemical and biophysical characterization of a truncated NADH dehydrogenase-2 of Escherichia coli; XLI Reunião Anual da Sociedade Brasileira de Bioquímica e Biologia Molecular; Foz do Iguacu; Brasil; 2012; 1-1
CONICET Digital
CONICET
url http://hdl.handle.net/11336/235545
identifier_str_mv Biochemical and biophysical characterization of a truncated NADH dehydrogenase-2 of Escherichia coli; XLI Reunião Anual da Sociedade Brasileira de Bioquímica e Biologia Molecular; Foz do Iguacu; Brasil; 2012; 1-1
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www2.sbbq.org.br/reuniao/cdrom/ra2012/resumos/R9191.pdf
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dc.coverage.none.fl_str_mv Internacional
dc.publisher.none.fl_str_mv Sociedade Brasileira de Bioquímica e Biologia Molecular
publisher.none.fl_str_mv Sociedade Brasileira de Bioquímica e Biologia Molecular
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
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instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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