A Spectroscopic Study of the Temperature Induced Modifications on Ferredoxin Folding and Iron−Sulfur Moieties

Autores
Todorovich, Smilja; Leal, Sonia S.; Salgueiro, Carlos A.; Zebger, Ingo; Hildebrandt, Peter; Murgida, Daniel Horacio; Gomes, Claudia Mónica
Año de publicación
2007
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Thermal perturbation of the dicluster ferredoxin from Acidianus ambivalens was investigated employing a toolbox of spectroscopic methods. FTIR and visible CD were used for assessing changes of the secondary structure and coarse alterations of the [3Fe4S] and [4Fe4S] cluster moieties, respectively. Fine details of the disassembly of the metal centers were revealed by paramagnetic NMR and resonance Raman spectroscopy. Overall, thermally induced unfolding of AaFd is initiated with the loss of alpha-helical content at relatively low temperatures (T-m(app) similar to 44 degrees C, followed by the disruption of both iron-sulfur clusters (T-m(app) similar to 53-60 degrees C. The degradation of the metal centers triggers major structural changes on the protein matrix, including the loss of tertiary contacts (T-m(app) similar to 58 degrees C) and a change, rather than a significant net loss, of secondary structure (T-m(app) similar to 60 degrees C. This latter process triggers a secondary structure reorganization that is consistent with the formation of a molten globule state. The combined spectroscopic approach here reported illustrates how changes in the metalloprotein organization are intertwined with disassembly of the iron-sulfur centers, denoting the conformational interplay of the protein backbone with cofactors.
Fil: Todorovich, Smilja. Universidade Nova de Lisboa; Portugal
Fil: Leal, Sonia S.. Universidade Nova de Lisboa; Portugal
Fil: Salgueiro, Carlos A.. Universidade Nova de Lisboa; Portugal
Fil: Zebger, Ingo. Technische Universitat Berlin; Alemania
Fil: Hildebrandt, Peter. Universidade Nova de Lisboa; Portugal. Technische Universitat Berlin; Alemania
Fil: Murgida, Daniel Horacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina. Universidade Nova de Lisboa; Portugal
Fil: Gomes, Claudia Mónica. Universidade Nova de Lisboa; Portugal
Materia
Ferredoxin
Unfolding
Raman
NMR
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/103546
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/103546
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling A Spectroscopic Study of the Temperature Induced Modifications on Ferredoxin Folding and Iron−Sulfur MoietiesTodorovich, SmiljaLeal, Sonia S.Salgueiro, Carlos A.Zebger, IngoHildebrandt, PeterMurgida, Daniel HoracioGomes, Claudia MónicaFerredoxinUnfoldingRamanNMRhttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1Thermal perturbation of the dicluster ferredoxin from Acidianus ambivalens was investigated employing a toolbox of spectroscopic methods. FTIR and visible CD were used for assessing changes of the secondary structure and coarse alterations of the [3Fe4S] and [4Fe4S] cluster moieties, respectively. Fine details of the disassembly of the metal centers were revealed by paramagnetic NMR and resonance Raman spectroscopy. Overall, thermally induced unfolding of AaFd is initiated with the loss of alpha-helical content at relatively low temperatures (T-m(app) similar to 44 degrees C, followed by the disruption of both iron-sulfur clusters (T-m(app) similar to 53-60 degrees C. The degradation of the metal centers triggers major structural changes on the protein matrix, including the loss of tertiary contacts (T-m(app) similar to 58 degrees C) and a change, rather than a significant net loss, of secondary structure (T-m(app) similar to 60 degrees C. This latter process triggers a secondary structure reorganization that is consistent with the formation of a molten globule state. The combined spectroscopic approach here reported illustrates how changes in the metalloprotein organization are intertwined with disassembly of the iron-sulfur centers, denoting the conformational interplay of the protein backbone with cofactors.Fil: Todorovich, Smilja. Universidade Nova de Lisboa; PortugalFil: Leal, Sonia S.. Universidade Nova de Lisboa; PortugalFil: Salgueiro, Carlos A.. Universidade Nova de Lisboa; PortugalFil: Zebger, Ingo. Technische Universitat Berlin; AlemaniaFil: Hildebrandt, Peter. Universidade Nova de Lisboa; Portugal. Technische Universitat Berlin; AlemaniaFil: Murgida, Daniel Horacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina. Universidade Nova de Lisboa; PortugalFil: Gomes, Claudia Mónica. Universidade Nova de Lisboa; PortugalAmerican Chemical Society2007-09info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/103546Todorovich, Smilja; Leal, Sonia S.; Salgueiro, Carlos A.; Zebger, Ingo; Hildebrandt, Peter; et al.; A Spectroscopic Study of the Temperature Induced Modifications on Ferredoxin Folding and Iron−Sulfur Moieties; American Chemical Society; Biochemistry; 46; 37; 9-2007; 10733-107380006-2960CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://pubs.acs.org/doi/abs/10.1021/bi700967ginfo:eu-repo/semantics/altIdentifier/doi/10.1021/bi700967ginfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:36:05Zoai:ri.conicet.gov.ar:11336/103546instacron: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:34982025-09-29 09:36:05.461CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv A Spectroscopic Study of the Temperature Induced Modifications on Ferredoxin Folding and Iron−Sulfur Moieties
title A Spectroscopic Study of the Temperature Induced Modifications on Ferredoxin Folding and Iron−Sulfur Moieties
spellingShingle A Spectroscopic Study of the Temperature Induced Modifications on Ferredoxin Folding and Iron−Sulfur Moieties
Todorovich, Smilja
Ferredoxin
Unfolding
Raman
NMR
title_short A Spectroscopic Study of the Temperature Induced Modifications on Ferredoxin Folding and Iron−Sulfur Moieties
title_full A Spectroscopic Study of the Temperature Induced Modifications on Ferredoxin Folding and Iron−Sulfur Moieties
title_fullStr A Spectroscopic Study of the Temperature Induced Modifications on Ferredoxin Folding and Iron−Sulfur Moieties
title_full_unstemmed A Spectroscopic Study of the Temperature Induced Modifications on Ferredoxin Folding and Iron−Sulfur Moieties
title_sort A Spectroscopic Study of the Temperature Induced Modifications on Ferredoxin Folding and Iron−Sulfur Moieties
dc.creator.none.fl_str_mv Todorovich, Smilja
Leal, Sonia S.
Salgueiro, Carlos A.
Zebger, Ingo
Hildebrandt, Peter
Murgida, Daniel Horacio
Gomes, Claudia Mónica
author Todorovich, Smilja
author_facet Todorovich, Smilja
Leal, Sonia S.
Salgueiro, Carlos A.
Zebger, Ingo
Hildebrandt, Peter
Murgida, Daniel Horacio
Gomes, Claudia Mónica
author_role author
author2 Leal, Sonia S.
Salgueiro, Carlos A.
Zebger, Ingo
Hildebrandt, Peter
Murgida, Daniel Horacio
Gomes, Claudia Mónica
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv Ferredoxin
Unfolding
Raman
NMR
topic Ferredoxin
Unfolding
Raman
NMR
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Thermal perturbation of the dicluster ferredoxin from Acidianus ambivalens was investigated employing a toolbox of spectroscopic methods. FTIR and visible CD were used for assessing changes of the secondary structure and coarse alterations of the [3Fe4S] and [4Fe4S] cluster moieties, respectively. Fine details of the disassembly of the metal centers were revealed by paramagnetic NMR and resonance Raman spectroscopy. Overall, thermally induced unfolding of AaFd is initiated with the loss of alpha-helical content at relatively low temperatures (T-m(app) similar to 44 degrees C, followed by the disruption of both iron-sulfur clusters (T-m(app) similar to 53-60 degrees C. The degradation of the metal centers triggers major structural changes on the protein matrix, including the loss of tertiary contacts (T-m(app) similar to 58 degrees C) and a change, rather than a significant net loss, of secondary structure (T-m(app) similar to 60 degrees C. This latter process triggers a secondary structure reorganization that is consistent with the formation of a molten globule state. The combined spectroscopic approach here reported illustrates how changes in the metalloprotein organization are intertwined with disassembly of the iron-sulfur centers, denoting the conformational interplay of the protein backbone with cofactors.
Fil: Todorovich, Smilja. Universidade Nova de Lisboa; Portugal
Fil: Leal, Sonia S.. Universidade Nova de Lisboa; Portugal
Fil: Salgueiro, Carlos A.. Universidade Nova de Lisboa; Portugal
Fil: Zebger, Ingo. Technische Universitat Berlin; Alemania
Fil: Hildebrandt, Peter. Universidade Nova de Lisboa; Portugal. Technische Universitat Berlin; Alemania
Fil: Murgida, Daniel Horacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina. Universidade Nova de Lisboa; Portugal
Fil: Gomes, Claudia Mónica. Universidade Nova de Lisboa; Portugal
description Thermal perturbation of the dicluster ferredoxin from Acidianus ambivalens was investigated employing a toolbox of spectroscopic methods. FTIR and visible CD were used for assessing changes of the secondary structure and coarse alterations of the [3Fe4S] and [4Fe4S] cluster moieties, respectively. Fine details of the disassembly of the metal centers were revealed by paramagnetic NMR and resonance Raman spectroscopy. Overall, thermally induced unfolding of AaFd is initiated with the loss of alpha-helical content at relatively low temperatures (T-m(app) similar to 44 degrees C, followed by the disruption of both iron-sulfur clusters (T-m(app) similar to 53-60 degrees C. The degradation of the metal centers triggers major structural changes on the protein matrix, including the loss of tertiary contacts (T-m(app) similar to 58 degrees C) and a change, rather than a significant net loss, of secondary structure (T-m(app) similar to 60 degrees C. This latter process triggers a secondary structure reorganization that is consistent with the formation of a molten globule state. The combined spectroscopic approach here reported illustrates how changes in the metalloprotein organization are intertwined with disassembly of the iron-sulfur centers, denoting the conformational interplay of the protein backbone with cofactors.
publishDate 2007
dc.date.none.fl_str_mv 2007-09
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/103546
Todorovich, Smilja; Leal, Sonia S.; Salgueiro, Carlos A.; Zebger, Ingo; Hildebrandt, Peter; et al.; A Spectroscopic Study of the Temperature Induced Modifications on Ferredoxin Folding and Iron−Sulfur Moieties; American Chemical Society; Biochemistry; 46; 37; 9-2007; 10733-10738
0006-2960
CONICET Digital
CONICET
url http://hdl.handle.net/11336/103546
identifier_str_mv Todorovich, Smilja; Leal, Sonia S.; Salgueiro, Carlos A.; Zebger, Ingo; Hildebrandt, Peter; et al.; A Spectroscopic Study of the Temperature Induced Modifications on Ferredoxin Folding and Iron−Sulfur Moieties; American Chemical Society; Biochemistry; 46; 37; 9-2007; 10733-10738
0006-2960
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://pubs.acs.org/doi/abs/10.1021/bi700967g
info:eu-repo/semantics/altIdentifier/doi/10.1021/bi700967g
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv American Chemical Society
publisher.none.fl_str_mv American Chemical Society
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
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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score 13.070432

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