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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| Format: | Online |
| Language: | English |
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Public Library of Science
2012
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| Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3513292/ |
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pubmed-3513292 |
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pubmed-35132922012-12-05 Biophysical Characterisation of Neuroglobin of the Icefish, a Natural Knockout for Hemoglobin and Myoglobin. Comparison with Human Neuroglobin Giordano, Daniela Boron, Ignacio Abbruzzetti, Stefania Van Leuven, Wendy Nicoletti, Francesco P. Forti, Flavio Bruno, Stefano Cheng, C-H. Christina Moens, Luc di Prisco, Guido Nadra, Alejandro D. Estrin, Darío Smulevich, Giulietta Dewilde, Sylvia Viappiani, Cristiano Verde, Cinzia Research Article 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. Public Library of Science 2012-12-03 /pmc/articles/PMC3513292/ /pubmed/23226490 http://dx.doi.org/10.1371/journal.pone.0044508 Text en © 2012 Giordano et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
| repository_type |
Open Access Journal |
| institution_category |
Foreign Institution |
| institution |
US National Center for Biotechnology Information |
| building |
NCBI PubMed |
| collection |
Online Access |
| language |
English |
| format |
Online |
| author |
Giordano, Daniela Boron, Ignacio Abbruzzetti, Stefania Van Leuven, Wendy Nicoletti, Francesco P. Forti, Flavio Bruno, Stefano Cheng, C-H. Christina Moens, Luc di Prisco, Guido Nadra, Alejandro D. Estrin, Darío Smulevich, Giulietta Dewilde, Sylvia Viappiani, Cristiano Verde, Cinzia |
| spellingShingle |
Giordano, Daniela Boron, Ignacio Abbruzzetti, Stefania Van Leuven, Wendy Nicoletti, Francesco P. Forti, Flavio Bruno, Stefano Cheng, C-H. Christina Moens, Luc di Prisco, Guido Nadra, Alejandro D. Estrin, Darío Smulevich, Giulietta Dewilde, Sylvia Viappiani, Cristiano Verde, Cinzia Biophysical Characterisation of Neuroglobin of the Icefish, a Natural Knockout for Hemoglobin and Myoglobin. Comparison with Human Neuroglobin |
| author_facet |
Giordano, Daniela Boron, Ignacio Abbruzzetti, Stefania Van Leuven, Wendy Nicoletti, Francesco P. Forti, Flavio Bruno, Stefano Cheng, C-H. Christina Moens, Luc di Prisco, Guido Nadra, Alejandro D. Estrin, Darío Smulevich, Giulietta Dewilde, Sylvia Viappiani, Cristiano Verde, Cinzia |
| author_sort |
Giordano, Daniela |
| 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 |
| 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. |
| publisher |
Public Library of Science |
| publishDate |
2012 |
| url |
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3513292/ |
| _version_ |
1611937782241951744 |