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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/66678
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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 Técnicas2025-09-29T09:54:23Zoai: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:34982025-09-29 09:54:23.512CONICET 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 |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/doi/10.1371/journal.pone.0044508 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) 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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1844613652407123968 |
score |
13.070432 |