Biophysical Characterisation of Neuroglobin of the Icefish, a Natural Knockout for Hemoglobin and Myoglobin. Comparison with Human Neuroglobin
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 t...
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2012
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| Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_19326203_v7_n12_p_Giordano http://repositoriouba.sisbi.uba.ar/gsdl/cgi-bin/library.cgi?a=d&c=artiaex&d=paper_19326203_v7_n12_p_Giordano_oai |
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I28-R145-paper_19326203_v7_n12_p_Giordano_oai2020-10-19 Giordano, D. Boron, I. Abbruzzetti, S. van Leuven, W. Nicoletti, F.P. Forti, F. Bruno, S. Cheng, C.-H.C. Moens, L. di Prisco, G. Nadra, A.D. Estrin, D. Smulevich, G. Dewilde, S. Viappiani, C. Verde, C. 2012 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 Fe 2+ 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:Nadra, A.D. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Estrin, D. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. application/pdf http://hdl.handle.net/20.500.12110/paper_19326203_v7_n12_p_Giordano info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar PLoS ONE 2012;7(12) hemoglobin myoglobin neuroglobin article autooxidation biophysics Chaenocephalus aceratus controlled study Dissostichus mawsoni fish human human versus animal comparison laser flash photolysis molecular cloning molecular dynamics nonhuman oxygen affinity oxygen transport photolysis protein analysis protein expression protein function protein purification protein structure Raman spectrometry site directed mutagenesis ultraviolet spectroscopy Animals Biophysics Carbon Monoxide Fishes Gene Knockout Techniques Globins Hemoglobins Humans Kinetics Ligands Molecular Dynamics Simulation Mutagenesis, Site-Directed Nerve Tissue Proteins Spectrophotometry, Ultraviolet Spectrum Analysis, Raman Chaenocephalus aceratus Dissostichus mawsoni Vertebrata Biophysical Characterisation of Neuroglobin of the Icefish, a Natural Knockout for Hemoglobin and Myoglobin. Comparison with Human Neuroglobin info:eu-repo/semantics/article info:ar-repo/semantics/artículo info:eu-repo/semantics/publishedVersion http://repositoriouba.sisbi.uba.ar/gsdl/cgi-bin/library.cgi?a=d&c=artiaex&d=paper_19326203_v7_n12_p_Giordano_oai |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-145 |
| collection |
Repositorio Digital de la Universidad de Buenos Aires (UBA) |
| topic |
hemoglobin myoglobin neuroglobin article autooxidation biophysics Chaenocephalus aceratus controlled study Dissostichus mawsoni fish human human versus animal comparison laser flash photolysis molecular cloning molecular dynamics nonhuman oxygen affinity oxygen transport photolysis protein analysis protein expression protein function protein purification protein structure Raman spectrometry site directed mutagenesis ultraviolet spectroscopy Animals Biophysics Carbon Monoxide Fishes Gene Knockout Techniques Globins Hemoglobins Humans Kinetics Ligands Molecular Dynamics Simulation Mutagenesis, Site-Directed Nerve Tissue Proteins Spectrophotometry, Ultraviolet Spectrum Analysis, Raman Chaenocephalus aceratus Dissostichus mawsoni Vertebrata |
| spellingShingle |
hemoglobin myoglobin neuroglobin article autooxidation biophysics Chaenocephalus aceratus controlled study Dissostichus mawsoni fish human human versus animal comparison laser flash photolysis molecular cloning molecular dynamics nonhuman oxygen affinity oxygen transport photolysis protein analysis protein expression protein function protein purification protein structure Raman spectrometry site directed mutagenesis ultraviolet spectroscopy Animals Biophysics Carbon Monoxide Fishes Gene Knockout Techniques Globins Hemoglobins Humans Kinetics Ligands Molecular Dynamics Simulation Mutagenesis, Site-Directed Nerve Tissue Proteins Spectrophotometry, Ultraviolet Spectrum Analysis, Raman Chaenocephalus aceratus Dissostichus mawsoni Vertebrata Giordano, D. Boron, I. Abbruzzetti, S. van Leuven, W. Nicoletti, F.P. Forti, F. Bruno, S. Cheng, C.-H.C. Moens, L. di Prisco, G. Nadra, A.D. Estrin, D. Smulevich, G. Dewilde, S. Viappiani, C. Verde, C. Biophysical Characterisation of Neuroglobin of the Icefish, a Natural Knockout for Hemoglobin and Myoglobin. Comparison with Human Neuroglobin |
| topic_facet |
hemoglobin myoglobin neuroglobin article autooxidation biophysics Chaenocephalus aceratus controlled study Dissostichus mawsoni fish human human versus animal comparison laser flash photolysis molecular cloning molecular dynamics nonhuman oxygen affinity oxygen transport photolysis protein analysis protein expression protein function protein purification protein structure Raman spectrometry site directed mutagenesis ultraviolet spectroscopy Animals Biophysics Carbon Monoxide Fishes Gene Knockout Techniques Globins Hemoglobins Humans Kinetics Ligands Molecular Dynamics Simulation Mutagenesis, Site-Directed Nerve Tissue Proteins Spectrophotometry, Ultraviolet Spectrum Analysis, Raman Chaenocephalus aceratus Dissostichus mawsoni Vertebrata |
| 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 Fe 2+ 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. |
| format |
Artículo Artículo publishedVersion |
| author |
Giordano, D. Boron, I. Abbruzzetti, S. van Leuven, W. Nicoletti, F.P. Forti, F. Bruno, S. Cheng, C.-H.C. Moens, L. di Prisco, G. Nadra, A.D. Estrin, D. Smulevich, G. Dewilde, S. Viappiani, C. Verde, C. |
| author_facet |
Giordano, D. Boron, I. Abbruzzetti, S. van Leuven, W. Nicoletti, F.P. Forti, F. Bruno, S. Cheng, C.-H.C. Moens, L. di Prisco, G. Nadra, A.D. Estrin, D. Smulevich, G. Dewilde, S. Viappiani, C. Verde, C. |
| author_sort |
Giordano, D. |
| title |
Biophysical Characterisation of Neuroglobin of the Icefish, a Natural Knockout for Hemoglobin and Myoglobin. Comparison with Human 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 |
| publishDate |
2012 |
| url |
http://hdl.handle.net/20.500.12110/paper_19326203_v7_n12_p_Giordano http://repositoriouba.sisbi.uba.ar/gsdl/cgi-bin/library.cgi?a=d&c=artiaex&d=paper_19326203_v7_n12_p_Giordano_oai |
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