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dc.contributor.author
Todorovich, Smilja
dc.contributor.author
Leal, Sonia S.
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Salgueiro, Carlos A.
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Zebger, Ingo
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Hildebrandt, Peter
dc.contributor.author
Murgida, Daniel Horacio
dc.contributor.author
Gomes, Claudia Mónica
dc.date.available
2020-04-24T15:44:00Z
dc.date.issued
2007-09
dc.identifier.citation
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
dc.identifier.issn
0006-2960
dc.identifier.uri
http://hdl.handle.net/11336/103546
dc.description.abstract
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.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
American Chemical Society
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Ferredoxin
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Unfolding
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Raman
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NMR
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Físico-Química, Ciencia de los Polímeros, Electroquímica
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Ciencias Químicas
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CIENCIAS NATURALES Y EXACTAS
dc.title
A Spectroscopic Study of the Temperature Induced Modifications on Ferredoxin Folding and Iron−Sulfur Moieties
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2020-04-22T15:40:38Z
dc.journal.volume
46
dc.journal.number
37
dc.journal.pagination
10733-10738
dc.journal.pais
Estados Unidos
dc.description.fil
Fil: Todorovich, Smilja. Universidade Nova de Lisboa; Portugal
dc.description.fil
Fil: Leal, Sonia S.. Universidade Nova de Lisboa; Portugal
dc.description.fil
Fil: Salgueiro, Carlos A.. Universidade Nova de Lisboa; Portugal
dc.description.fil
Fil: Zebger, Ingo. Technische Universitat Berlin; Alemania
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Fil: Hildebrandt, Peter. Universidade Nova de Lisboa; Portugal. Technische Universitat Berlin; Alemania
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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
dc.description.fil
Fil: Gomes, Claudia Mónica. Universidade Nova de Lisboa; Portugal
dc.journal.title
Biochemistry
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://pubs.acs.org/doi/abs/10.1021/bi700967g
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1021/bi700967g
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