On the stability of the extracellular hemoglobin of Glossoscolex paulistus, in two iron oxidation states, in the presence of urea
Autor(a) principal: | |
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Data de Publicação: | 2012 |
Outros Autores: | , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNESP |
Texto Completo: | http://dx.doi.org/10.1016/j.abb.2012.01.007 http://hdl.handle.net/11449/42634 |
Resumo: | The stability of the Glossoscolex paulistus hemoglobin (HbGp), in two iron oxidation states (and three forms), as monitored by optical absorption, fluorescence emission and circular dichroism (CD) spectroscopies, in the presence of the chaotropic agent urea, is studied. HbGp oligomeric dissociation, denaturation and iron oxidation are observed. CD data show that the cyanomet-HbGp is more stable than the oxy-form. Oxy- and cyanomet-HbGp show good fits on the basis of a two state model with critical urea concentrations at 220-222 nm of 5.1 +/- 0.2 and 6.1 +/- 0.1 mol/L, respectively. The three-state model was able to reveal a subtle second transition at lower urea concentration (1.0-2.0 mol/L) associated to partial oligomeric dissociation. The intermediate state for oxy- and cyanomet-HbGp is very similar to the native state. For met-HbGp, a different equilibrium, in the presence of urea, is observed. A sharp transition at 1.95 +/- 0.05 mol/L of denaturant is observed, associated to oligomeric dissociation and hemichrome formation. In this case, analysis by a three-state model reveals the great similarity between the intermediate and the unfolded states. Analysis of spectroscopic data, by two-state and three-state models, reveals consistency of obtained thermodynamic parameters for HbGp urea denaturation. (C) 2012 Elsevier B.V. All rights reserved. |
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Repositório Institucional da UNESP |
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On the stability of the extracellular hemoglobin of Glossoscolex paulistus, in two iron oxidation states, in the presence of ureaUreaOptical absorptionFluorescence emissionCircular dichroismGlossoscolex paulistusThree-state model and oligomeric stabilityThe stability of the Glossoscolex paulistus hemoglobin (HbGp), in two iron oxidation states (and three forms), as monitored by optical absorption, fluorescence emission and circular dichroism (CD) spectroscopies, in the presence of the chaotropic agent urea, is studied. HbGp oligomeric dissociation, denaturation and iron oxidation are observed. CD data show that the cyanomet-HbGp is more stable than the oxy-form. Oxy- and cyanomet-HbGp show good fits on the basis of a two state model with critical urea concentrations at 220-222 nm of 5.1 +/- 0.2 and 6.1 +/- 0.1 mol/L, respectively. The three-state model was able to reveal a subtle second transition at lower urea concentration (1.0-2.0 mol/L) associated to partial oligomeric dissociation. The intermediate state for oxy- and cyanomet-HbGp is very similar to the native state. For met-HbGp, a different equilibrium, in the presence of urea, is observed. A sharp transition at 1.95 +/- 0.05 mol/L of denaturant is observed, associated to oligomeric dissociation and hemichrome formation. In this case, analysis by a three-state model reveals the great similarity between the intermediate and the unfolded states. Analysis of spectroscopic data, by two-state and three-state models, reveals consistency of obtained thermodynamic parameters for HbGp urea denaturation. (C) 2012 Elsevier B.V. All rights reserved.Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)Univ São Paulo, Inst Quim São Carlos, São Paulo, BrazilUniv Estadual Paulista Julio de Mesquita Filho Re, São Paulo, BrazilUniv Estadual Paulista Julio de Mesquita Filho Re, São Paulo, BrazilFAPESP: 09/17261-6Elsevier B.V.Universidade de São Paulo (USP)Universidade Estadual Paulista (Unesp)Carvalho, Francisco Adriano O.Santiago, Patricia S. [UNESP]Tabak, Marcel2014-05-20T15:34:43Z2014-05-20T15:34:43Z2012-03-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article46-58application/pdfhttp://dx.doi.org/10.1016/j.abb.2012.01.007Archives of Biochemistry and Biophysics. New York: Elsevier B.V., v. 519, n. 1, p. 46-58, 2012.0003-9861http://hdl.handle.net/11449/4263410.1016/j.abb.2012.01.007WOS:000301028300007WOS000301028300007.pdf67053670106620870000-0002-6205-9441Web of Sciencereponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengArchives of Biochemistry and Biophysics3.1181,350info:eu-repo/semantics/openAccess2023-12-20T06:23:57Zoai:repositorio.unesp.br:11449/42634Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T20:50:09.101620Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
On the stability of the extracellular hemoglobin of Glossoscolex paulistus, in two iron oxidation states, in the presence of urea |
title |
On the stability of the extracellular hemoglobin of Glossoscolex paulistus, in two iron oxidation states, in the presence of urea |
spellingShingle |
On the stability of the extracellular hemoglobin of Glossoscolex paulistus, in two iron oxidation states, in the presence of urea Carvalho, Francisco Adriano O. Urea Optical absorption Fluorescence emission Circular dichroism Glossoscolex paulistus Three-state model and oligomeric stability |
title_short |
On the stability of the extracellular hemoglobin of Glossoscolex paulistus, in two iron oxidation states, in the presence of urea |
title_full |
On the stability of the extracellular hemoglobin of Glossoscolex paulistus, in two iron oxidation states, in the presence of urea |
title_fullStr |
On the stability of the extracellular hemoglobin of Glossoscolex paulistus, in two iron oxidation states, in the presence of urea |
title_full_unstemmed |
On the stability of the extracellular hemoglobin of Glossoscolex paulistus, in two iron oxidation states, in the presence of urea |
title_sort |
On the stability of the extracellular hemoglobin of Glossoscolex paulistus, in two iron oxidation states, in the presence of urea |
author |
Carvalho, Francisco Adriano O. |
author_facet |
Carvalho, Francisco Adriano O. Santiago, Patricia S. [UNESP] Tabak, Marcel |
author_role |
author |
author2 |
Santiago, Patricia S. [UNESP] Tabak, Marcel |
author2_role |
author author |
dc.contributor.none.fl_str_mv |
Universidade de São Paulo (USP) Universidade Estadual Paulista (Unesp) |
dc.contributor.author.fl_str_mv |
Carvalho, Francisco Adriano O. Santiago, Patricia S. [UNESP] Tabak, Marcel |
dc.subject.por.fl_str_mv |
Urea Optical absorption Fluorescence emission Circular dichroism Glossoscolex paulistus Three-state model and oligomeric stability |
topic |
Urea Optical absorption Fluorescence emission Circular dichroism Glossoscolex paulistus Three-state model and oligomeric stability |
description |
The stability of the Glossoscolex paulistus hemoglobin (HbGp), in two iron oxidation states (and three forms), as monitored by optical absorption, fluorescence emission and circular dichroism (CD) spectroscopies, in the presence of the chaotropic agent urea, is studied. HbGp oligomeric dissociation, denaturation and iron oxidation are observed. CD data show that the cyanomet-HbGp is more stable than the oxy-form. Oxy- and cyanomet-HbGp show good fits on the basis of a two state model with critical urea concentrations at 220-222 nm of 5.1 +/- 0.2 and 6.1 +/- 0.1 mol/L, respectively. The three-state model was able to reveal a subtle second transition at lower urea concentration (1.0-2.0 mol/L) associated to partial oligomeric dissociation. The intermediate state for oxy- and cyanomet-HbGp is very similar to the native state. For met-HbGp, a different equilibrium, in the presence of urea, is observed. A sharp transition at 1.95 +/- 0.05 mol/L of denaturant is observed, associated to oligomeric dissociation and hemichrome formation. In this case, analysis by a three-state model reveals the great similarity between the intermediate and the unfolded states. Analysis of spectroscopic data, by two-state and three-state models, reveals consistency of obtained thermodynamic parameters for HbGp urea denaturation. (C) 2012 Elsevier B.V. All rights reserved. |
publishDate |
2012 |
dc.date.none.fl_str_mv |
2012-03-01 2014-05-20T15:34:43Z 2014-05-20T15:34:43Z |
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://dx.doi.org/10.1016/j.abb.2012.01.007 Archives of Biochemistry and Biophysics. New York: Elsevier B.V., v. 519, n. 1, p. 46-58, 2012. 0003-9861 http://hdl.handle.net/11449/42634 10.1016/j.abb.2012.01.007 WOS:000301028300007 WOS000301028300007.pdf 6705367010662087 0000-0002-6205-9441 |
url |
http://dx.doi.org/10.1016/j.abb.2012.01.007 http://hdl.handle.net/11449/42634 |
identifier_str_mv |
Archives of Biochemistry and Biophysics. New York: Elsevier B.V., v. 519, n. 1, p. 46-58, 2012. 0003-9861 10.1016/j.abb.2012.01.007 WOS:000301028300007 WOS000301028300007.pdf 6705367010662087 0000-0002-6205-9441 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Archives of Biochemistry and Biophysics 3.118 1,350 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
46-58 application/pdf |
dc.publisher.none.fl_str_mv |
Elsevier B.V. |
publisher.none.fl_str_mv |
Elsevier B.V. |
dc.source.none.fl_str_mv |
Web of Science reponame:Repositório Institucional da UNESP instname:Universidade Estadual Paulista (UNESP) instacron:UNESP |
instname_str |
Universidade Estadual Paulista (UNESP) |
instacron_str |
UNESP |
institution |
UNESP |
reponame_str |
Repositório Institucional da UNESP |
collection |
Repositório Institucional da UNESP |
repository.name.fl_str_mv |
Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP) |
repository.mail.fl_str_mv |
|
_version_ |
1808129256304148480 |