Desulfovibrio gigas ferredoxin II: redox structural modulation of the [3Fe–4S] cluster
Autor(a) principal: | |
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Data de Publicação: | 2006 |
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/10362/8710 |
Resumo: | J Biol Inorg Chem (2006) 11: 307–315 DOI 10.1007/s00775-005-0077-2 |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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7160 |
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Desulfovibrio gigas ferredoxin II: redox structural modulation of the [3Fe–4S] clusterJ Biol Inorg Chem (2006) 11: 307–315 DOI 10.1007/s00775-005-0077-2Desulfovibrio gigas ferredoxin II (DgFdII) is a small protein with a polypeptide chain composed of 58 amino acids, containing one Fe3S4 cluster per monomer. Upon studying the redox cycle of this protein, we detected a stable intermediate (FdIIint) with four 1H resonances at 24.1, 20.5, 20.8 and 13.7 ppm. The differences between FdIIox and FdIIint were attributed to conformational changes resulting from the breaking/formation of an internal disulfide bridge. The same 1H NMR methodology used to fully assign the three cysteinyl ligands of the [3Fe-4S] core in the oxidized state (DgFdIIox) was used here for the assignment of the same three ligands in the intermediate state (DgFdIIint). The spin-coupling model used for the oxidized form of DgFdII where magnetic exchange coupling constants of around 300 cm-1 and hyperfine coupling constants equal to 1 MHz for all the three iron centres were found, does not explain the isotropic shift temperature dependence for the three cysteinyl cluster ligands in DgFdIIint. This study, together with the spin delocalization mechanism proposed here for DgFdIIint, allows the detection of structural modifications at the [3Fe-4S] cluster in DgFdIIox and DgFdIIint.SpringerRUNRodrigues, Pedro M.Macedo, Anjos L.Moura, IsabelMoura, José J. G.Goodfellow, Brian J.2013-02-06T11:45:46Z20062006-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10362/8710eng0949-8257info: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:RCAAP2024-03-11T03:41:36Zoai:run.unl.pt:10362/8710Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T03:18:23.513819Repositório 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 |
Desulfovibrio gigas ferredoxin II: redox structural modulation of the [3Fe–4S] cluster |
title |
Desulfovibrio gigas ferredoxin II: redox structural modulation of the [3Fe–4S] cluster |
spellingShingle |
Desulfovibrio gigas ferredoxin II: redox structural modulation of the [3Fe–4S] cluster Rodrigues, Pedro M. |
title_short |
Desulfovibrio gigas ferredoxin II: redox structural modulation of the [3Fe–4S] cluster |
title_full |
Desulfovibrio gigas ferredoxin II: redox structural modulation of the [3Fe–4S] cluster |
title_fullStr |
Desulfovibrio gigas ferredoxin II: redox structural modulation of the [3Fe–4S] cluster |
title_full_unstemmed |
Desulfovibrio gigas ferredoxin II: redox structural modulation of the [3Fe–4S] cluster |
title_sort |
Desulfovibrio gigas ferredoxin II: redox structural modulation of the [3Fe–4S] cluster |
author |
Rodrigues, Pedro M. |
author_facet |
Rodrigues, Pedro M. Macedo, Anjos L. Moura, Isabel Moura, José J. G. Goodfellow, Brian J. |
author_role |
author |
author2 |
Macedo, Anjos L. Moura, Isabel Moura, José J. G. Goodfellow, Brian J. |
author2_role |
author author author author |
dc.contributor.none.fl_str_mv |
RUN |
dc.contributor.author.fl_str_mv |
Rodrigues, Pedro M. Macedo, Anjos L. Moura, Isabel Moura, José J. G. Goodfellow, Brian J. |
description |
J Biol Inorg Chem (2006) 11: 307–315 DOI 10.1007/s00775-005-0077-2 |
publishDate |
2006 |
dc.date.none.fl_str_mv |
2006 2006-01-01T00:00:00Z 2013-02-06T11:45:46Z |
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/10362/8710 |
url |
http://hdl.handle.net/10362/8710 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
0949-8257 |
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.publisher.none.fl_str_mv |
Springer |
publisher.none.fl_str_mv |
Springer |
dc.source.none.fl_str_mv |
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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 |
reponame_str |
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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