Computational Study of Iron(II) and -(III) Complexes with a Simple Model Human H Ferritin Ferroxidase Center

Autores
Bacelo, Daniel Enrique; Binning, R. C.
Año de publicación
2006
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Interaction of iron ions with a six-amino acid model of the ferroxidase center of human H chain ferritin has been examined in density functional theory calculations. The model, based on experimental studies of oxidation of Fe2+ at the center, consists of Glu27, Glu62, His65, Glu107, Gln141, and Ala144. Reasonable structures are obtained in a survey of types of iron complexes inferred to occur in the ferroxidase reaction. Structures of complexes of the model center with one and two Fe2+ ions, with diiron(III) bridged by peroxide and bridged by oxide-peroxide combinations, have been optimized. Calculations on diiron(III) complexes confirm that stable peroxide-bridged complexes can form and that the Fe-Fe distance in at least one is consistent with the experimental Fe-Fe distance observed in the blue peroxodiferric complex of ferritin.2+ at the center, consists of Glu27, Glu62, His65, Glu107, Gln141, and Ala144. Reasonable structures are obtained in a survey of types of iron complexes inferred to occur in the ferroxidase reaction. Structures of complexes of the model center with one and two Fe2+ ions, with diiron(III) bridged by peroxide and bridged by oxide-peroxide combinations, have been optimized. Calculations on diiron(III) complexes confirm that stable peroxide-bridged complexes can form and that the Fe-Fe distance in at least one is consistent with the experimental Fe-Fe distance observed in the blue peroxodiferric complex of ferritin.
Fil: Bacelo, Daniel Enrique. Universidad Nacional de la Patagonia "San Juan Bosco"; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Binning, R. C.. Universidad Metropolitana; Venezuela
Materia
Fe2+
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:11336/244680
Acceder
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network_name_str CONICET Digital (CONICET)
spelling Computational Study of Iron(II) and -(III) Complexes with a Simple Model Human H Ferritin Ferroxidase CenterBacelo, Daniel EnriqueBinning, R. C.Fe2+https://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1Interaction of iron ions with a six-amino acid model of the ferroxidase center of human H chain ferritin has been examined in density functional theory calculations. The model, based on experimental studies of oxidation of Fe2+ at the center, consists of Glu27, Glu62, His65, Glu107, Gln141, and Ala144. Reasonable structures are obtained in a survey of types of iron complexes inferred to occur in the ferroxidase reaction. Structures of complexes of the model center with one and two Fe2+ ions, with diiron(III) bridged by peroxide and bridged by oxide-peroxide combinations, have been optimized. Calculations on diiron(III) complexes confirm that stable peroxide-bridged complexes can form and that the Fe-Fe distance in at least one is consistent with the experimental Fe-Fe distance observed in the blue peroxodiferric complex of ferritin.2+ at the center, consists of Glu27, Glu62, His65, Glu107, Gln141, and Ala144. Reasonable structures are obtained in a survey of types of iron complexes inferred to occur in the ferroxidase reaction. Structures of complexes of the model center with one and two Fe2+ ions, with diiron(III) bridged by peroxide and bridged by oxide-peroxide combinations, have been optimized. Calculations on diiron(III) complexes confirm that stable peroxide-bridged complexes can form and that the Fe-Fe distance in at least one is consistent with the experimental Fe-Fe distance observed in the blue peroxodiferric complex of ferritin.Fil: Bacelo, Daniel Enrique. Universidad Nacional de la Patagonia "San Juan Bosco"; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Binning, R. C.. Universidad Metropolitana; VenezuelaAmerican Chemical Society2006-11info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/244680Bacelo, Daniel Enrique; Binning, R. C.; Computational Study of Iron(II) and -(III) Complexes with a Simple Model Human H Ferritin Ferroxidase Center; American Chemical Society; Inorganic Chemistry; 45; 25; 11-2006; 10263-102690020-1669CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://pubs.acs.org/doi/10.1021/ic060388kinfo:eu-repo/semantics/altIdentifier/doi/10.1021/ic060388kinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-12-23T13:37:00Zoai:ri.conicet.gov.ar:11336/244680instacron: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:34982025-12-23 13:37:01.172CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Computational Study of Iron(II) and -(III) Complexes with a Simple Model Human H Ferritin Ferroxidase Center
title Computational Study of Iron(II) and -(III) Complexes with a Simple Model Human H Ferritin Ferroxidase Center
spellingShingle Computational Study of Iron(II) and -(III) Complexes with a Simple Model Human H Ferritin Ferroxidase Center
Bacelo, Daniel Enrique
Fe2+
title_short Computational Study of Iron(II) and -(III) Complexes with a Simple Model Human H Ferritin Ferroxidase Center
title_full Computational Study of Iron(II) and -(III) Complexes with a Simple Model Human H Ferritin Ferroxidase Center
title_fullStr Computational Study of Iron(II) and -(III) Complexes with a Simple Model Human H Ferritin Ferroxidase Center
title_full_unstemmed Computational Study of Iron(II) and -(III) Complexes with a Simple Model Human H Ferritin Ferroxidase Center
title_sort Computational Study of Iron(II) and -(III) Complexes with a Simple Model Human H Ferritin Ferroxidase Center
dc.creator.none.fl_str_mv Bacelo, Daniel Enrique
Binning, R. C.
author Bacelo, Daniel Enrique
author_facet Bacelo, Daniel Enrique
Binning, R. C.
author_role author
author2 Binning, R. C.
author2_role author
dc.subject.none.fl_str_mv Fe2+
topic Fe2+
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Interaction of iron ions with a six-amino acid model of the ferroxidase center of human H chain ferritin has been examined in density functional theory calculations. The model, based on experimental studies of oxidation of Fe2+ at the center, consists of Glu27, Glu62, His65, Glu107, Gln141, and Ala144. Reasonable structures are obtained in a survey of types of iron complexes inferred to occur in the ferroxidase reaction. Structures of complexes of the model center with one and two Fe2+ ions, with diiron(III) bridged by peroxide and bridged by oxide-peroxide combinations, have been optimized. Calculations on diiron(III) complexes confirm that stable peroxide-bridged complexes can form and that the Fe-Fe distance in at least one is consistent with the experimental Fe-Fe distance observed in the blue peroxodiferric complex of ferritin.2+ at the center, consists of Glu27, Glu62, His65, Glu107, Gln141, and Ala144. Reasonable structures are obtained in a survey of types of iron complexes inferred to occur in the ferroxidase reaction. Structures of complexes of the model center with one and two Fe2+ ions, with diiron(III) bridged by peroxide and bridged by oxide-peroxide combinations, have been optimized. Calculations on diiron(III) complexes confirm that stable peroxide-bridged complexes can form and that the Fe-Fe distance in at least one is consistent with the experimental Fe-Fe distance observed in the blue peroxodiferric complex of ferritin.
Fil: Bacelo, Daniel Enrique. Universidad Nacional de la Patagonia "San Juan Bosco"; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Binning, R. C.. Universidad Metropolitana; Venezuela
description Interaction of iron ions with a six-amino acid model of the ferroxidase center of human H chain ferritin has been examined in density functional theory calculations. The model, based on experimental studies of oxidation of Fe2+ at the center, consists of Glu27, Glu62, His65, Glu107, Gln141, and Ala144. Reasonable structures are obtained in a survey of types of iron complexes inferred to occur in the ferroxidase reaction. Structures of complexes of the model center with one and two Fe2+ ions, with diiron(III) bridged by peroxide and bridged by oxide-peroxide combinations, have been optimized. Calculations on diiron(III) complexes confirm that stable peroxide-bridged complexes can form and that the Fe-Fe distance in at least one is consistent with the experimental Fe-Fe distance observed in the blue peroxodiferric complex of ferritin.2+ at the center, consists of Glu27, Glu62, His65, Glu107, Gln141, and Ala144. Reasonable structures are obtained in a survey of types of iron complexes inferred to occur in the ferroxidase reaction. Structures of complexes of the model center with one and two Fe2+ ions, with diiron(III) bridged by peroxide and bridged by oxide-peroxide combinations, have been optimized. Calculations on diiron(III) complexes confirm that stable peroxide-bridged complexes can form and that the Fe-Fe distance in at least one is consistent with the experimental Fe-Fe distance observed in the blue peroxodiferric complex of ferritin.
publishDate 2006
dc.date.none.fl_str_mv 2006-11
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/11336/244680
Bacelo, Daniel Enrique; Binning, R. C.; Computational Study of Iron(II) and -(III) Complexes with a Simple Model Human H Ferritin Ferroxidase Center; American Chemical Society; Inorganic Chemistry; 45; 25; 11-2006; 10263-10269
0020-1669
CONICET Digital
CONICET
url http://hdl.handle.net/11336/244680
identifier_str_mv Bacelo, Daniel Enrique; Binning, R. C.; Computational Study of Iron(II) and -(III) Complexes with a Simple Model Human H Ferritin Ferroxidase Center; American Chemical Society; Inorganic Chemistry; 45; 25; 11-2006; 10263-10269
0020-1669
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://pubs.acs.org/doi/10.1021/ic060388k
info:eu-repo/semantics/altIdentifier/doi/10.1021/ic060388k
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
dc.publisher.none.fl_str_mv American Chemical Society
publisher.none.fl_str_mv American Chemical Society
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 13.075124

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