Structural stability of adenylate kinase from the sulfate-reducing bacteria Desulfovibrio gigas

Detalhes bibliográficos
Autor(a) principal: Moura, José J. G.
Data de Publicação: 2004
Outros Autores: Moura, Isabel, Gavel, Olga Yu., Bursakov, Sergey A., Pina, David G., Zhadan, Galina G., Shnyrov, Valery L.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10362/1535
Resumo: Biophysical Chemistry 110 (2004) 83–92
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spelling Structural stability of adenylate kinase from the sulfate-reducing bacteria Desulfovibrio gigasProtein stabilityDifferential scanning calorimetryCircular dichroismIntrinsic fluorescenceAdenylate kinaseDesulfovibrio gigasBiophysical Chemistry 110 (2004) 83–92A novel adenylate kinase (AK) has recently been purified from Desulfovibrio gigas and characterized as a Co2+/Zn2+-containing enzyme: this is an unusual characteristic for AKs from Gram-negative bacteria, in which these enzymes are normally devoid of metals. Here, we studied the conformational stability of holo- and apo-AK as a function of temperature by differential scanning calorimetry (DSC), circular dichroism (CD), and intrinsic fluorescence spectroscopy. The thermal unfolding of AK is a cooperative two-state process, and is sufficiently reversible in the 9–11 pH range, that can be correctly interpreted in terms of a simple two-state thermodynamic model. The spectral parameters as monitored by ellipticity changes in the CD spectra of the enzyme as well as the decrease in tryptophan intensity emission upon heating were seen to be good complements to the highly sensitive but integral DSC-method.supported in part by the Fundação para a Ciência e a Tecnologia, Portugal, fellowships BD/13775/97 to OYG, BPD/3518/00 to SAB, SFRH/BD/1067/2000 to DGP, and NATO Scientific Programme Fellowships for Spain, call 2002 to GGZ.ElsevierRUNMoura, José J. G.Moura, IsabelGavel, Olga Yu.Bursakov, Sergey A.Pina, David G.Zhadan, Galina G.Shnyrov, Valery L.2008-07-30T11:04:34Z2004-042004-04-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10362/1535eng0301-4622info: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:RCAAP2024-03-11T03:31:33Zoai:run.unl.pt:10362/1535Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T03:14:44.975086Repositório 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 Structural stability of adenylate kinase from the sulfate-reducing bacteria Desulfovibrio gigas
title Structural stability of adenylate kinase from the sulfate-reducing bacteria Desulfovibrio gigas
spellingShingle Structural stability of adenylate kinase from the sulfate-reducing bacteria Desulfovibrio gigas
Moura, José J. G.
Protein stability
Differential scanning calorimetry
Circular dichroism
Intrinsic fluorescence
Adenylate kinase
Desulfovibrio gigas
title_short Structural stability of adenylate kinase from the sulfate-reducing bacteria Desulfovibrio gigas
title_full Structural stability of adenylate kinase from the sulfate-reducing bacteria Desulfovibrio gigas
title_fullStr Structural stability of adenylate kinase from the sulfate-reducing bacteria Desulfovibrio gigas
title_full_unstemmed Structural stability of adenylate kinase from the sulfate-reducing bacteria Desulfovibrio gigas
title_sort Structural stability of adenylate kinase from the sulfate-reducing bacteria Desulfovibrio gigas
author Moura, José J. G.
author_facet Moura, José J. G.
Moura, Isabel
Gavel, Olga Yu.
Bursakov, Sergey A.
Pina, David G.
Zhadan, Galina G.
Shnyrov, Valery L.
author_role author
author2 Moura, Isabel
Gavel, Olga Yu.
Bursakov, Sergey A.
Pina, David G.
Zhadan, Galina G.
Shnyrov, Valery L.
author2_role author
author
author
author
author
author
dc.contributor.none.fl_str_mv RUN
dc.contributor.author.fl_str_mv Moura, José J. G.
Moura, Isabel
Gavel, Olga Yu.
Bursakov, Sergey A.
Pina, David G.
Zhadan, Galina G.
Shnyrov, Valery L.
dc.subject.por.fl_str_mv Protein stability
Differential scanning calorimetry
Circular dichroism
Intrinsic fluorescence
Adenylate kinase
Desulfovibrio gigas
topic Protein stability
Differential scanning calorimetry
Circular dichroism
Intrinsic fluorescence
Adenylate kinase
Desulfovibrio gigas
description Biophysical Chemistry 110 (2004) 83–92
publishDate 2004
dc.date.none.fl_str_mv 2004-04
2004-04-01T00:00:00Z
2008-07-30T11:04:34Z
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/10362/1535
url http://hdl.handle.net/10362/1535
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 0301-4622
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 Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron:RCAAP
instname_str Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
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reponame_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
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repository.name.fl_str_mv Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
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