Molecular basis of the NO trans influence in quaternary T-state human hemoglobin: A computational study

Autores
Petruk, Ariel Alcides; Vergara, Alessandro; Estrin, Dario Ariel; Merlino, Antonello
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
NO binding to the T-state of human hemoglobin (HbA) induces the cleavage of the proximal His bonds to the heme iron in the α-chains, whereas it leaves the β-hemes hexacoordinated. The structure of the nitrosylated T-state of the W37Eβ mutant (W37E) shows that the Fe-His87α bond remains intact. Exactly how mutation affects NO binding and why tension is apparent only in HbA α-heme remains to be elucidated. By means of density functional theory electronic structure calculations and classical molecular dynamics simulations we provide an explanation for the poorly understood NO binding properties of HbA and its W37E mutant. The data suggest an interplay between electronic effects, tertiary structure and hydration site modifications in determining the tension in the NO-ligated T-state HbA α-chain.
Fil: Petruk, Ariel Alcides. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina. Universidad de Buenos Aires; Argentina
Fil: Vergara, Alessandro. University of Naples "Federico II".Department of Chemical Sciences; Italia. Consiglio Nazionale delle Ricerche. Institute of Biostructures and Bioimages; Italia
Fil: Estrin, Dario Ariel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina. Universidad de Buenos Aires; Argentina
Fil: Merlino, Antonello. Consiglio Nazionale delle Ricerche. Institute of Biostructures and Bioimages; Italia. University of Naples "Federico II".Department of Chemical Sciences; Italia
Materia
Hemoglobin
Dft
Qm-Mm
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/8280
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/8280
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Molecular basis of the NO trans influence in quaternary T-state human hemoglobin: A computational studyPetruk, Ariel AlcidesVergara, AlessandroEstrin, Dario ArielMerlino, AntonelloHemoglobinDftQm-Mmhttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1NO binding to the T-state of human hemoglobin (HbA) induces the cleavage of the proximal His bonds to the heme iron in the α-chains, whereas it leaves the β-hemes hexacoordinated. The structure of the nitrosylated T-state of the W37Eβ mutant (W37E) shows that the Fe-His87α bond remains intact. Exactly how mutation affects NO binding and why tension is apparent only in HbA α-heme remains to be elucidated. By means of density functional theory electronic structure calculations and classical molecular dynamics simulations we provide an explanation for the poorly understood NO binding properties of HbA and its W37E mutant. The data suggest an interplay between electronic effects, tertiary structure and hydration site modifications in determining the tension in the NO-ligated T-state HbA α-chain.Fil: Petruk, Ariel Alcides. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina. Universidad de Buenos Aires; ArgentinaFil: Vergara, Alessandro. University of Naples "Federico II".Department of Chemical Sciences; Italia. Consiglio Nazionale delle Ricerche. Institute of Biostructures and Bioimages; ItaliaFil: Estrin, Dario Ariel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina. Universidad de Buenos Aires; ArgentinaFil: Merlino, Antonello. Consiglio Nazionale delle Ricerche. Institute of Biostructures and Bioimages; Italia. University of Naples "Federico II".Department of Chemical Sciences; ItaliaElsevier2013-06-13info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/8280Petruk, Ariel Alcides; Vergara, Alessandro; Estrin, Dario Ariel; Merlino, Antonello; Molecular basis of the NO trans influence in quaternary T-state human hemoglobin: A computational study; Elsevier; Febs Letters; 587; 15; 13-6-2013; 2393-23980014-5793enginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.febslet.2013.06.006info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0014579313004511info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-10T13:08:13Zoai:ri.conicet.gov.ar:11336/8280instacron: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:34982025-09-10 13:08:13.964CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Molecular basis of the NO trans influence in quaternary T-state human hemoglobin: A computational study
title Molecular basis of the NO trans influence in quaternary T-state human hemoglobin: A computational study
spellingShingle Molecular basis of the NO trans influence in quaternary T-state human hemoglobin: A computational study
Petruk, Ariel Alcides
Hemoglobin
Dft
Qm-Mm
title_short Molecular basis of the NO trans influence in quaternary T-state human hemoglobin: A computational study
title_full Molecular basis of the NO trans influence in quaternary T-state human hemoglobin: A computational study
title_fullStr Molecular basis of the NO trans influence in quaternary T-state human hemoglobin: A computational study
title_full_unstemmed Molecular basis of the NO trans influence in quaternary T-state human hemoglobin: A computational study
title_sort Molecular basis of the NO trans influence in quaternary T-state human hemoglobin: A computational study
dc.creator.none.fl_str_mv Petruk, Ariel Alcides
Vergara, Alessandro
Estrin, Dario Ariel
Merlino, Antonello
author Petruk, Ariel Alcides
author_facet Petruk, Ariel Alcides
Vergara, Alessandro
Estrin, Dario Ariel
Merlino, Antonello
author_role author
author2 Vergara, Alessandro
Estrin, Dario Ariel
Merlino, Antonello
author2_role author
author
author
dc.subject.none.fl_str_mv Hemoglobin
Dft
Qm-Mm
topic Hemoglobin
Dft
Qm-Mm
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv NO binding to the T-state of human hemoglobin (HbA) induces the cleavage of the proximal His bonds to the heme iron in the α-chains, whereas it leaves the β-hemes hexacoordinated. The structure of the nitrosylated T-state of the W37Eβ mutant (W37E) shows that the Fe-His87α bond remains intact. Exactly how mutation affects NO binding and why tension is apparent only in HbA α-heme remains to be elucidated. By means of density functional theory electronic structure calculations and classical molecular dynamics simulations we provide an explanation for the poorly understood NO binding properties of HbA and its W37E mutant. The data suggest an interplay between electronic effects, tertiary structure and hydration site modifications in determining the tension in the NO-ligated T-state HbA α-chain.
Fil: Petruk, Ariel Alcides. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina. Universidad de Buenos Aires; Argentina
Fil: Vergara, Alessandro. University of Naples "Federico II".Department of Chemical Sciences; Italia. Consiglio Nazionale delle Ricerche. Institute of Biostructures and Bioimages; Italia
Fil: Estrin, Dario Ariel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina. Universidad de Buenos Aires; Argentina
Fil: Merlino, Antonello. Consiglio Nazionale delle Ricerche. Institute of Biostructures and Bioimages; Italia. University of Naples "Federico II".Department of Chemical Sciences; Italia
description NO binding to the T-state of human hemoglobin (HbA) induces the cleavage of the proximal His bonds to the heme iron in the α-chains, whereas it leaves the β-hemes hexacoordinated. The structure of the nitrosylated T-state of the W37Eβ mutant (W37E) shows that the Fe-His87α bond remains intact. Exactly how mutation affects NO binding and why tension is apparent only in HbA α-heme remains to be elucidated. By means of density functional theory electronic structure calculations and classical molecular dynamics simulations we provide an explanation for the poorly understood NO binding properties of HbA and its W37E mutant. The data suggest an interplay between electronic effects, tertiary structure and hydration site modifications in determining the tension in the NO-ligated T-state HbA α-chain.
publishDate 2013
dc.date.none.fl_str_mv 2013-06-13
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/11336/8280
Petruk, Ariel Alcides; Vergara, Alessandro; Estrin, Dario Ariel; Merlino, Antonello; Molecular basis of the NO trans influence in quaternary T-state human hemoglobin: A computational study; Elsevier; Febs Letters; 587; 15; 13-6-2013; 2393-2398
0014-5793
url http://hdl.handle.net/11336/8280
identifier_str_mv Petruk, Ariel Alcides; Vergara, Alessandro; Estrin, Dario Ariel; Merlino, Antonello; Molecular basis of the NO trans influence in quaternary T-state human hemoglobin: A computational study; Elsevier; Febs Letters; 587; 15; 13-6-2013; 2393-2398
0014-5793
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1016/j.febslet.2013.06.006
info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0014579313004511
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
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 12.993085

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