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dc.contributor.author
Giordano, Daniela
dc.contributor.author
Boron, Carlos Ignacio
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Abbruzzetti, Stefania
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van Leuven, Wendy
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Nicoletti, Francesco P.
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Forti, Flavio
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Bruno, Stefano
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Cheng, C. H. Christina
dc.contributor.author
Moens, Luc
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di Prisco, Guido
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Nadra, Alejandro Daniel
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Estrin, Dario Ariel
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Smulevich, Giulietta
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Dewilde, Sylvia
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Viappiani, Cristiano
dc.contributor.author
Verde, Cinzia
dc.date.available
2018-12-18T18:28:53Z
dc.date.issued
2012-12
dc.identifier.citation
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
dc.identifier.issn
1932-6203
dc.identifier.uri
http://hdl.handle.net/11336/66678
dc.description.abstract
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.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Public Library of Science
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Hemoglobin
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Neuroglobin
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Otras Ciencias Químicas
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Ciencias Químicas
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CIENCIAS NATURALES Y EXACTAS
dc.title
Biophysical Characterisation of Neuroglobin of the Icefish, a Natural Knockout for Hemoglobin and Myoglobin. Comparison with Human Neuroglobin
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2018-11-05T19:15:13Z
dc.journal.volume
7
dc.journal.number
12
dc.journal.pagination
1-10
dc.journal.pais
Estados Unidos
dc.journal.ciudad
San Francisco
dc.description.fil
Fil: Giordano, Daniela. Institute of Protein Biochemistry; Italia
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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
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Fil: Abbruzzetti, Stefania. Università di Parma; Italia
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Fil: van Leuven, Wendy. Universiteit Antwerp; Bélgica
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Fil: Nicoletti, Francesco P.. Università degli Studi di Firenze; Italia
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Fil: Forti, Flavio. Universidad de Barcelona; España
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Fil: Bruno, Stefano. Università di Parma; Italia
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Fil: Cheng, C. H. Christina. University of Illinois at Urbana; Estados Unidos
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Fil: Moens, Luc. Universiteit Antwerp; Bélgica
dc.description.fil
Fil: di Prisco, Guido. Institute of Protein Biochemistry; Italia
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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
dc.description.fil
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
dc.description.fil
Fil: Smulevich, Giulietta. Università degli Studi di Firenze; Italia
dc.description.fil
Fil: Dewilde, Sylvia. Universiteit Antwerp; Bélgica
dc.description.fil
Fil: Viappiani, Cristiano. Università di Parma; Italia
dc.description.fil
Fil: Verde, Cinzia. Institute of Protein Biochemistry; Italia
dc.journal.title
Plos One
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/https://doi.org/10.1371/journal.pone.0044508
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0044508
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