A full conformational space analysis of bilirubin

Autores
Vega Hissi, Esteban Gabriel; Garro Martinez, Juan Ceferino; Zamarbide, Graciela Nidia; Estrada, Mario Rinaldo; Knak Jensen, Svend J.; Tomas Vert, Francisco; Csizmadia, Imre G.
Año de publicación
2009
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Ab initio methods were utilized in a gas-phase systematic conformational search of bilirubin conformers. The whole molecule was divided into four fragments. Most stable conformers of them were employed to build 196 conformers of the complete bilirubin molecule. Initial geometries were optimized using HF/321Glevel of theory and the minimum energy conformerswere then reoptimized at B3LYP/6-31G(d) level. Ridge-tile conformer was the most stable one, in perfect agreement with X-ray data. We found that while tetrapyrrole backbone shows some flexibility, propionic acid side chains have a greater influence in bilirubin conformation because they can interact through different hydrogen bond patterns with the backbone and between them.
Fil: Vega Hissi, Esteban Gabriel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis; Argentina. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia. Departamento de Farmacia; Argentina
Fil: Garro Martinez, Juan Ceferino. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis; Argentina. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia. Departamento de Farmacia; Argentina
Fil: Zamarbide, Graciela Nidia. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia. Departamento de Farmacia; Argentina
Fil: Estrada, Mario Rinaldo. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia. Departamento de Farmacia; Argentina
Fil: Knak Jensen, Svend J.. University Aarhus; Dinamarca
Fil: Tomas Vert, Francisco. Universidad de Valencia; España
Fil: Csizmadia, Imre G.. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia. Departamento de Farmacia; Argentina. University of Toronto; Canadá. University of Szeged. Department of Chemistry and Chemical Informatics. Faculty of Education; Hungría
Materia
BILIRRUBIN
RIDGE-TILE
HYDROGEN BOND PATTERN
FLEXIBILITY
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/158403
Acceder
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repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling A full conformational space analysis of bilirubinVega Hissi, Esteban GabrielGarro Martinez, Juan CeferinoZamarbide, Graciela NidiaEstrada, Mario RinaldoKnak Jensen, Svend J.Tomas Vert, FranciscoCsizmadia, Imre G.BILIRRUBINRIDGE-TILEHYDROGEN BOND PATTERNFLEXIBILITYhttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1Ab initio methods were utilized in a gas-phase systematic conformational search of bilirubin conformers. The whole molecule was divided into four fragments. Most stable conformers of them were employed to build 196 conformers of the complete bilirubin molecule. Initial geometries were optimized using HF/321Glevel of theory and the minimum energy conformerswere then reoptimized at B3LYP/6-31G(d) level. Ridge-tile conformer was the most stable one, in perfect agreement with X-ray data. We found that while tetrapyrrole backbone shows some flexibility, propionic acid side chains have a greater influence in bilirubin conformation because they can interact through different hydrogen bond patterns with the backbone and between them.Fil: Vega Hissi, Esteban Gabriel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis; Argentina. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia. Departamento de Farmacia; ArgentinaFil: Garro Martinez, Juan Ceferino. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis; Argentina. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia. Departamento de Farmacia; ArgentinaFil: Zamarbide, Graciela Nidia. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia. Departamento de Farmacia; ArgentinaFil: Estrada, Mario Rinaldo. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia. Departamento de Farmacia; ArgentinaFil: Knak Jensen, Svend J.. University Aarhus; DinamarcaFil: Tomas Vert, Francisco. Universidad de Valencia; EspañaFil: Csizmadia, Imre G.. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia. Departamento de Farmacia; Argentina. University of Toronto; Canadá. University of Szeged. Department of Chemistry and Chemical Informatics. Faculty of Education; HungríaElsevier Science2009-10info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/158403Vega Hissi, Esteban Gabriel; Garro Martinez, Juan Ceferino; Zamarbide, Graciela Nidia; Estrada, Mario Rinaldo; Knak Jensen, Svend J.; et al.; A full conformational space analysis of bilirubin; Elsevier Science; Journal of Molecular Structure Theochem; 911; 1-3; 10-2009; 24-290166-1280CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/abs/pii/S0166128009004345info:eu-repo/semantics/altIdentifier/doi/10.1016/j.theochem.2009.06.039info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:33:37Zoai:ri.conicet.gov.ar:11336/158403instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 09:33:37.572CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv A full conformational space analysis of bilirubin
title A full conformational space analysis of bilirubin
spellingShingle A full conformational space analysis of bilirubin
Vega Hissi, Esteban Gabriel
BILIRRUBIN
RIDGE-TILE
HYDROGEN BOND PATTERN
FLEXIBILITY
title_short A full conformational space analysis of bilirubin
title_full A full conformational space analysis of bilirubin
title_fullStr A full conformational space analysis of bilirubin
title_full_unstemmed A full conformational space analysis of bilirubin
title_sort A full conformational space analysis of bilirubin
dc.creator.none.fl_str_mv Vega Hissi, Esteban Gabriel
Garro Martinez, Juan Ceferino
Zamarbide, Graciela Nidia
Estrada, Mario Rinaldo
Knak Jensen, Svend J.
Tomas Vert, Francisco
Csizmadia, Imre G.
author Vega Hissi, Esteban Gabriel
author_facet Vega Hissi, Esteban Gabriel
Garro Martinez, Juan Ceferino
Zamarbide, Graciela Nidia
Estrada, Mario Rinaldo
Knak Jensen, Svend J.
Tomas Vert, Francisco
Csizmadia, Imre G.
author_role author
author2 Garro Martinez, Juan Ceferino
Zamarbide, Graciela Nidia
Estrada, Mario Rinaldo
Knak Jensen, Svend J.
Tomas Vert, Francisco
Csizmadia, Imre G.
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv BILIRRUBIN
RIDGE-TILE
HYDROGEN BOND PATTERN
FLEXIBILITY
topic BILIRRUBIN
RIDGE-TILE
HYDROGEN BOND PATTERN
FLEXIBILITY
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Ab initio methods were utilized in a gas-phase systematic conformational search of bilirubin conformers. The whole molecule was divided into four fragments. Most stable conformers of them were employed to build 196 conformers of the complete bilirubin molecule. Initial geometries were optimized using HF/321Glevel of theory and the minimum energy conformerswere then reoptimized at B3LYP/6-31G(d) level. Ridge-tile conformer was the most stable one, in perfect agreement with X-ray data. We found that while tetrapyrrole backbone shows some flexibility, propionic acid side chains have a greater influence in bilirubin conformation because they can interact through different hydrogen bond patterns with the backbone and between them.
Fil: Vega Hissi, Esteban Gabriel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis; Argentina. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia. Departamento de Farmacia; Argentina
Fil: Garro Martinez, Juan Ceferino. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis; Argentina. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia. Departamento de Farmacia; Argentina
Fil: Zamarbide, Graciela Nidia. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia. Departamento de Farmacia; Argentina
Fil: Estrada, Mario Rinaldo. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia. Departamento de Farmacia; Argentina
Fil: Knak Jensen, Svend J.. University Aarhus; Dinamarca
Fil: Tomas Vert, Francisco. Universidad de Valencia; España
Fil: Csizmadia, Imre G.. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia. Departamento de Farmacia; Argentina. University of Toronto; Canadá. University of Szeged. Department of Chemistry and Chemical Informatics. Faculty of Education; Hungría
description Ab initio methods were utilized in a gas-phase systematic conformational search of bilirubin conformers. The whole molecule was divided into four fragments. Most stable conformers of them were employed to build 196 conformers of the complete bilirubin molecule. Initial geometries were optimized using HF/321Glevel of theory and the minimum energy conformerswere then reoptimized at B3LYP/6-31G(d) level. Ridge-tile conformer was the most stable one, in perfect agreement with X-ray data. We found that while tetrapyrrole backbone shows some flexibility, propionic acid side chains have a greater influence in bilirubin conformation because they can interact through different hydrogen bond patterns with the backbone and between them.
publishDate 2009
dc.date.none.fl_str_mv 2009-10
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/158403
Vega Hissi, Esteban Gabriel; Garro Martinez, Juan Ceferino; Zamarbide, Graciela Nidia; Estrada, Mario Rinaldo; Knak Jensen, Svend J.; et al.; A full conformational space analysis of bilirubin; Elsevier Science; Journal of Molecular Structure Theochem; 911; 1-3; 10-2009; 24-29
0166-1280
CONICET Digital
CONICET
url http://hdl.handle.net/11336/158403
identifier_str_mv Vega Hissi, Esteban Gabriel; Garro Martinez, Juan Ceferino; Zamarbide, Graciela Nidia; Estrada, Mario Rinaldo; Knak Jensen, Svend J.; et al.; A full conformational space analysis of bilirubin; Elsevier Science; Journal of Molecular Structure Theochem; 911; 1-3; 10-2009; 24-29
0166-1280
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/abs/pii/S0166128009004345
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.theochem.2009.06.039
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier Science
publisher.none.fl_str_mv Elsevier Science
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.070432

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