Molecular determinants for FMN-binding in Desulfovibrio gigas flavoredoxin
Autor(a) principal: | |
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Data de Publicação: | 2007 |
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/10174/1577 |
Resumo: | Abstract: Flavoredoxin participates in Desulfovibrio gigas thiosulfate reduction pathway. Its 3-dimensional model was generated allowing the oxidized riboflavin-5'-phosphate (FMN) site to be predicted. Residues likely to be involved in FMN-binding were identified (N29, W35, T56, K92, H131 and F164) and mutated to alanine. Fluorescence titration with apoprotein showed that FMN is strongly bound in the wild-type protein. Comparison of K-d values for mutants suggests that interactions with the phosphate group of FMN, contribute more to binding than the interactions with the isoalloxazine ring. The redox potential of bound FMN determined for wild-type and mutants revealed shifts to less negative values. These findings were correlated with the protein structure in order to contribute to a better understanding of the structure-function relationships in flavoredoxin. (c) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. |
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Molecular determinants for FMN-binding in Desulfovibrio gigas flavoredoxinDesulfovibrio gigasflavoredoxinAbstract: Flavoredoxin participates in Desulfovibrio gigas thiosulfate reduction pathway. Its 3-dimensional model was generated allowing the oxidized riboflavin-5'-phosphate (FMN) site to be predicted. Residues likely to be involved in FMN-binding were identified (N29, W35, T56, K92, H131 and F164) and mutated to alanine. Fluorescence titration with apoprotein showed that FMN is strongly bound in the wild-type protein. Comparison of K-d values for mutants suggests that interactions with the phosphate group of FMN, contribute more to binding than the interactions with the isoalloxazine ring. The redox potential of bound FMN determined for wild-type and mutants revealed shifts to less negative values. These findings were correlated with the protein structure in order to contribute to a better understanding of the structure-function relationships in flavoredoxin. (c) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.2009-04-15T15:43:15Z2009-04-152007-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article35871 bytesapplication/pdfhttp://hdl.handle.net/10174/1577http://hdl.handle.net/10174/1577engpag 4397-4402FEBS LETTERS23581livrendndndndnd365Broco, ManuelaSoares, Claudio M.Oliveira, SolangeMayhew, Stephen GRodrigues-Pousada, Claudinainfo: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:RCAAP2024-01-03T18:37:17Zoai:dspace.uevora.pt:10174/1577Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T00:57:27.043166Repositório 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 |
Molecular determinants for FMN-binding in Desulfovibrio gigas flavoredoxin |
title |
Molecular determinants for FMN-binding in Desulfovibrio gigas flavoredoxin |
spellingShingle |
Molecular determinants for FMN-binding in Desulfovibrio gigas flavoredoxin Broco, Manuela Desulfovibrio gigas flavoredoxin |
title_short |
Molecular determinants for FMN-binding in Desulfovibrio gigas flavoredoxin |
title_full |
Molecular determinants for FMN-binding in Desulfovibrio gigas flavoredoxin |
title_fullStr |
Molecular determinants for FMN-binding in Desulfovibrio gigas flavoredoxin |
title_full_unstemmed |
Molecular determinants for FMN-binding in Desulfovibrio gigas flavoredoxin |
title_sort |
Molecular determinants for FMN-binding in Desulfovibrio gigas flavoredoxin |
author |
Broco, Manuela |
author_facet |
Broco, Manuela Soares, Claudio M. Oliveira, Solange Mayhew, Stephen G Rodrigues-Pousada, Claudina |
author_role |
author |
author2 |
Soares, Claudio M. Oliveira, Solange Mayhew, Stephen G Rodrigues-Pousada, Claudina |
author2_role |
author author author author |
dc.contributor.author.fl_str_mv |
Broco, Manuela Soares, Claudio M. Oliveira, Solange Mayhew, Stephen G Rodrigues-Pousada, Claudina |
dc.subject.por.fl_str_mv |
Desulfovibrio gigas flavoredoxin |
topic |
Desulfovibrio gigas flavoredoxin |
description |
Abstract: Flavoredoxin participates in Desulfovibrio gigas thiosulfate reduction pathway. Its 3-dimensional model was generated allowing the oxidized riboflavin-5'-phosphate (FMN) site to be predicted. Residues likely to be involved in FMN-binding were identified (N29, W35, T56, K92, H131 and F164) and mutated to alanine. Fluorescence titration with apoprotein showed that FMN is strongly bound in the wild-type protein. Comparison of K-d values for mutants suggests that interactions with the phosphate group of FMN, contribute more to binding than the interactions with the isoalloxazine ring. The redox potential of bound FMN determined for wild-type and mutants revealed shifts to less negative values. These findings were correlated with the protein structure in order to contribute to a better understanding of the structure-function relationships in flavoredoxin. (c) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. |
publishDate |
2007 |
dc.date.none.fl_str_mv |
2007-01-01T00:00:00Z 2009-04-15T15:43:15Z 2009-04-15 |
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/10174/1577 http://hdl.handle.net/10174/1577 |
url |
http://hdl.handle.net/10174/1577 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
pag 4397-4402 FEBS LETTERS 23 581 livre nd nd nd nd nd 365 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
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35871 bytes application/pdf |
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Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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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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