Biophysical Characterisation of Neuroglobin of the Icefish, a Natural Knockout for Hemoglobin and Myoglobin. Comparison with Human Neuroglobin

Autores
Giordano, Daniela; Boron, Carlos Ignacio; Abbruzzetti, Stefania; van Leuven, Wendy; Nicoletti, Francesco P.; Forti, Flavio; Bruno, Stefano; Cheng, C. H. Christina; Moens, Luc; di Prisco, Guido; Nadra, Alejandro Daniel; Estrin, Dario Ariel; Smulevich, Giulietta; Dewilde, Sylvia; Viappiani, Cristiano; Verde, Cinzia
Año de publicación
2012
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The Antarctic icefish Chaenocephalus aceratus lacks the globins common to most vertebrates, hemoglobin and myoglobin, but has retained neuroglobin in the brain. This conserved globin has been cloned, over-expressed and purified. To highlight similarities and differences, the structural features of the neuroglobin of this colourless-blooded fish were compared with those of the well characterised human neuroglobin as well as with the neuroglobin from the retina of the red blooded, hemoglobin and myoglobin-containing, closely related Antarctic notothenioid Dissostichus mawsoni. A detailed structural and functional analysis of the two Antarctic fish neuroglobins was carried out by UV-visible and Resonance Raman spectroscopies, molecular dynamics simulations and laser-flash photolysis. Similar to the human protein, Antarctic fish neuroglobins can reversibly bind oxygen and CO in the Fe2+ form, and show six-coordination by distal His in the absence of exogenous ligands. A very large and structured internal cavity, with discrete docking sites, was identified in the modelled three-dimensional structures of the Antarctic neuroglobins. Estimate of the free-energy barriers from laser-flash photolysis and Implicit Ligand Sampling showed that the cavities are accessible from the solvent in both proteins. Comparison of structural and functional properties suggests that the two Antarctic fish neuroglobins most likely preserved and possibly improved the function recently proposed for human neuroglobin in ligand multichemistry. Despite subtle differences, the adaptation of Antarctic fish neuroglobins does not seem to parallel the dramatic adaptation of the oxygen carrying globins, hemoglobin and myoglobin, in the same organisms. © 2012 Giordano et al.
Fil: Giordano, Daniela. Institute of Protein Biochemistry; Italia
Fil: Boron, Carlos Ignacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina
Fil: Abbruzzetti, Stefania. Università di Parma; Italia
Fil: van Leuven, Wendy. Universiteit Antwerp; Bélgica
Fil: Nicoletti, Francesco P.. Università degli Studi di Firenze; Italia
Fil: Forti, Flavio. Universidad de Barcelona; España
Fil: Bruno, Stefano. Università di Parma; Italia
Fil: Cheng, C. H. Christina. University of Illinois at Urbana; Estados Unidos
Fil: Moens, Luc. Universiteit Antwerp; Bélgica
Fil: di Prisco, Guido. Institute of Protein Biochemistry; Italia
Fil: Nadra, Alejandro Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Fisiología, Biología Molecular y Celular; Argentina
Fil: Estrin, Dario Ariel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina
Fil: Smulevich, Giulietta. Università degli Studi di Firenze; Italia
Fil: Dewilde, Sylvia. Universiteit Antwerp; Bélgica
Fil: Viappiani, Cristiano. Università di Parma; Italia
Fil: Verde, Cinzia. Institute of Protein Biochemistry; Italia
Materia
Hemoglobin
Neuroglobin
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:11336/66678
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/66678
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Biophysical Characterisation of Neuroglobin of the Icefish, a Natural Knockout for Hemoglobin and Myoglobin. Comparison with Human NeuroglobinGiordano, DanielaBoron, Carlos IgnacioAbbruzzetti, Stefaniavan Leuven, WendyNicoletti, Francesco P.Forti, FlavioBruno, StefanoCheng, C. H. ChristinaMoens, Lucdi Prisco, GuidoNadra, Alejandro DanielEstrin, Dario ArielSmulevich, GiuliettaDewilde, SylviaViappiani, CristianoVerde, CinziaHemoglobinNeuroglobinhttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1The Antarctic icefish Chaenocephalus aceratus lacks the globins common to most vertebrates, hemoglobin and myoglobin, but has retained neuroglobin in the brain. This conserved globin has been cloned, over-expressed and purified. To highlight similarities and differences, the structural features of the neuroglobin of this colourless-blooded fish were compared with those of the well characterised human neuroglobin as well as with the neuroglobin from the retina of the red blooded, hemoglobin and myoglobin-containing, closely related Antarctic notothenioid Dissostichus mawsoni. A detailed structural and functional analysis of the two Antarctic fish neuroglobins was carried out by UV-visible and Resonance Raman spectroscopies, molecular dynamics simulations and laser-flash photolysis. Similar to the human protein, Antarctic fish neuroglobins can reversibly bind oxygen and CO in the Fe2+ form, and show six-coordination by distal His in the absence of exogenous ligands. A very large and structured internal cavity, with discrete docking sites, was identified in the modelled three-dimensional structures of the Antarctic neuroglobins. Estimate of the free-energy barriers from laser-flash photolysis and Implicit Ligand Sampling showed that the cavities are accessible from the solvent in both proteins. Comparison of structural and functional properties suggests that the two Antarctic fish neuroglobins most likely preserved and possibly improved the function recently proposed for human neuroglobin in ligand multichemistry. Despite subtle differences, the adaptation of Antarctic fish neuroglobins does not seem to parallel the dramatic adaptation of the oxygen carrying globins, hemoglobin and myoglobin, in the same organisms. © 2012 Giordano et al.Fil: Giordano, Daniela. Institute of Protein Biochemistry; ItaliaFil: Boron, Carlos Ignacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; ArgentinaFil: Abbruzzetti, Stefania. Università di Parma; ItaliaFil: van Leuven, Wendy. Universiteit Antwerp; BélgicaFil: Nicoletti, Francesco P.. Università degli Studi di Firenze; ItaliaFil: Forti, Flavio. Universidad de Barcelona; EspañaFil: Bruno, Stefano. Università di Parma; ItaliaFil: Cheng, C. H. Christina. University of Illinois at Urbana; Estados UnidosFil: Moens, Luc. Universiteit Antwerp; BélgicaFil: di Prisco, Guido. Institute of Protein Biochemistry; ItaliaFil: Nadra, Alejandro Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Fisiología, Biología Molecular y Celular; ArgentinaFil: Estrin, Dario Ariel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; ArgentinaFil: Smulevich, Giulietta. Università degli Studi di Firenze; ItaliaFil: Dewilde, Sylvia. Universiteit Antwerp; BélgicaFil: Viappiani, Cristiano. Università di Parma; ItaliaFil: Verde, Cinzia. Institute of Protein Biochemistry; ItaliaPublic Library of Science2012-12info: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/11336/66678Giordano, Daniela; Boron, Carlos Ignacio; Abbruzzetti, Stefania; van Leuven, Wendy; Nicoletti, Francesco P.; et al.; Biophysical Characterisation of Neuroglobin of the Icefish, a Natural Knockout for Hemoglobin and Myoglobin. Comparison with Human Neuroglobin; Public Library of Science; Plos One; 7; 12; 12-2012; 1-101932-6203CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1371/journal.pone.0044508info:eu-repo/semantics/altIdentifier/url/https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0044508info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-29T11:53:36Zoai:ri.conicet.gov.ar:11336/66678instacron: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:34982025-10-29 11:53:37.246CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Biophysical Characterisation of Neuroglobin of the Icefish, a Natural Knockout for Hemoglobin and Myoglobin. Comparison with Human Neuroglobin
title Biophysical Characterisation of Neuroglobin of the Icefish, a Natural Knockout for Hemoglobin and Myoglobin. Comparison with Human Neuroglobin
spellingShingle Biophysical Characterisation of Neuroglobin of the Icefish, a Natural Knockout for Hemoglobin and Myoglobin. Comparison with Human Neuroglobin
Giordano, Daniela
Hemoglobin
Neuroglobin
title_short Biophysical Characterisation of Neuroglobin of the Icefish, a Natural Knockout for Hemoglobin and Myoglobin. Comparison with Human Neuroglobin
title_full Biophysical Characterisation of Neuroglobin of the Icefish, a Natural Knockout for Hemoglobin and Myoglobin. Comparison with Human Neuroglobin
title_fullStr Biophysical Characterisation of Neuroglobin of the Icefish, a Natural Knockout for Hemoglobin and Myoglobin. Comparison with Human Neuroglobin
title_full_unstemmed Biophysical Characterisation of Neuroglobin of the Icefish, a Natural Knockout for Hemoglobin and Myoglobin. Comparison with Human Neuroglobin
title_sort Biophysical Characterisation of Neuroglobin of the Icefish, a Natural Knockout for Hemoglobin and Myoglobin. Comparison with Human Neuroglobin
dc.creator.none.fl_str_mv Giordano, Daniela
Boron, Carlos Ignacio
Abbruzzetti, Stefania
van Leuven, Wendy
Nicoletti, Francesco P.
Forti, Flavio
Bruno, Stefano
Cheng, C. H. Christina
Moens, Luc
di Prisco, Guido
Nadra, Alejandro Daniel
Estrin, Dario Ariel
Smulevich, Giulietta
Dewilde, Sylvia
Viappiani, Cristiano
Verde, Cinzia
author Giordano, Daniela
author_facet Giordano, Daniela
Boron, Carlos Ignacio
Abbruzzetti, Stefania
van Leuven, Wendy
Nicoletti, Francesco P.
Forti, Flavio
Bruno, Stefano
Cheng, C. H. Christina
Moens, Luc
di Prisco, Guido
Nadra, Alejandro Daniel
Estrin, Dario Ariel
Smulevich, Giulietta
Dewilde, Sylvia
Viappiani, Cristiano
Verde, Cinzia
author_role author
author2 Boron, Carlos Ignacio
Abbruzzetti, Stefania
van Leuven, Wendy
Nicoletti, Francesco P.
Forti, Flavio
Bruno, Stefano
Cheng, C. H. Christina
Moens, Luc
di Prisco, Guido
Nadra, Alejandro Daniel
Estrin, Dario Ariel
Smulevich, Giulietta
Dewilde, Sylvia
Viappiani, Cristiano
Verde, Cinzia
author2_role author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Hemoglobin
Neuroglobin
topic Hemoglobin
Neuroglobin
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The Antarctic icefish Chaenocephalus aceratus lacks the globins common to most vertebrates, hemoglobin and myoglobin, but has retained neuroglobin in the brain. This conserved globin has been cloned, over-expressed and purified. To highlight similarities and differences, the structural features of the neuroglobin of this colourless-blooded fish were compared with those of the well characterised human neuroglobin as well as with the neuroglobin from the retina of the red blooded, hemoglobin and myoglobin-containing, closely related Antarctic notothenioid Dissostichus mawsoni. A detailed structural and functional analysis of the two Antarctic fish neuroglobins was carried out by UV-visible and Resonance Raman spectroscopies, molecular dynamics simulations and laser-flash photolysis. Similar to the human protein, Antarctic fish neuroglobins can reversibly bind oxygen and CO in the Fe2+ form, and show six-coordination by distal His in the absence of exogenous ligands. A very large and structured internal cavity, with discrete docking sites, was identified in the modelled three-dimensional structures of the Antarctic neuroglobins. Estimate of the free-energy barriers from laser-flash photolysis and Implicit Ligand Sampling showed that the cavities are accessible from the solvent in both proteins. Comparison of structural and functional properties suggests that the two Antarctic fish neuroglobins most likely preserved and possibly improved the function recently proposed for human neuroglobin in ligand multichemistry. Despite subtle differences, the adaptation of Antarctic fish neuroglobins does not seem to parallel the dramatic adaptation of the oxygen carrying globins, hemoglobin and myoglobin, in the same organisms. © 2012 Giordano et al.
Fil: Giordano, Daniela. Institute of Protein Biochemistry; Italia
Fil: Boron, Carlos Ignacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina
Fil: Abbruzzetti, Stefania. Università di Parma; Italia
Fil: van Leuven, Wendy. Universiteit Antwerp; Bélgica
Fil: Nicoletti, Francesco P.. Università degli Studi di Firenze; Italia
Fil: Forti, Flavio. Universidad de Barcelona; España
Fil: Bruno, Stefano. Università di Parma; Italia
Fil: Cheng, C. H. Christina. University of Illinois at Urbana; Estados Unidos
Fil: Moens, Luc. Universiteit Antwerp; Bélgica
Fil: di Prisco, Guido. Institute of Protein Biochemistry; Italia
Fil: Nadra, Alejandro Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Fisiología, Biología Molecular y Celular; Argentina
Fil: Estrin, Dario Ariel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina
Fil: Smulevich, Giulietta. Università degli Studi di Firenze; Italia
Fil: Dewilde, Sylvia. Universiteit Antwerp; Bélgica
Fil: Viappiani, Cristiano. Università di Parma; Italia
Fil: Verde, Cinzia. Institute of Protein Biochemistry; Italia
description The Antarctic icefish Chaenocephalus aceratus lacks the globins common to most vertebrates, hemoglobin and myoglobin, but has retained neuroglobin in the brain. This conserved globin has been cloned, over-expressed and purified. To highlight similarities and differences, the structural features of the neuroglobin of this colourless-blooded fish were compared with those of the well characterised human neuroglobin as well as with the neuroglobin from the retina of the red blooded, hemoglobin and myoglobin-containing, closely related Antarctic notothenioid Dissostichus mawsoni. A detailed structural and functional analysis of the two Antarctic fish neuroglobins was carried out by UV-visible and Resonance Raman spectroscopies, molecular dynamics simulations and laser-flash photolysis. Similar to the human protein, Antarctic fish neuroglobins can reversibly bind oxygen and CO in the Fe2+ form, and show six-coordination by distal His in the absence of exogenous ligands. A very large and structured internal cavity, with discrete docking sites, was identified in the modelled three-dimensional structures of the Antarctic neuroglobins. Estimate of the free-energy barriers from laser-flash photolysis and Implicit Ligand Sampling showed that the cavities are accessible from the solvent in both proteins. Comparison of structural and functional properties suggests that the two Antarctic fish neuroglobins most likely preserved and possibly improved the function recently proposed for human neuroglobin in ligand multichemistry. Despite subtle differences, the adaptation of Antarctic fish neuroglobins does not seem to parallel the dramatic adaptation of the oxygen carrying globins, hemoglobin and myoglobin, in the same organisms. © 2012 Giordano et al.
publishDate 2012
dc.date.none.fl_str_mv 2012-12
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/11336/66678
Giordano, Daniela; Boron, Carlos Ignacio; Abbruzzetti, Stefania; van Leuven, Wendy; Nicoletti, Francesco P.; et al.; Biophysical Characterisation of Neuroglobin of the Icefish, a Natural Knockout for Hemoglobin and Myoglobin. Comparison with Human Neuroglobin; Public Library of Science; Plos One; 7; 12; 12-2012; 1-10
1932-6203
CONICET Digital
CONICET
url http://hdl.handle.net/11336/66678
identifier_str_mv Giordano, Daniela; Boron, Carlos Ignacio; Abbruzzetti, Stefania; van Leuven, Wendy; Nicoletti, Francesco P.; et al.; Biophysical Characterisation of Neuroglobin of the Icefish, a Natural Knockout for Hemoglobin and Myoglobin. Comparison with Human Neuroglobin; Public Library of Science; Plos One; 7; 12; 12-2012; 1-10
1932-6203
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
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info:eu-repo/semantics/altIdentifier/url/https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0044508
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 Public Library of Science
publisher.none.fl_str_mv Public Library of Science
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
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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 13.10058

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