Biophysical characterisation of neuroglobin of the icefish, a natural knockout for hemoglobin and myoglobin : comparison with human neuroglobin
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 fea...
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ftunivantwerpen:c:irua:105973 2023-07-16T03:53:35+02:00 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 Moens, Luc Dewilde, Sylvia 2012 pdf https://hdl.handle.net/10067/1059730151162165141 https://repository.uantwerpen.be/docman/irua/686265/3910.pdf eng eng info:eu-repo/semantics/altIdentifier/doi/10.1371/JOURNAL.PONE.0044508 info:eu-repo/semantics/altIdentifier/isi/000312104700001 info:eu-repo/semantics/openAccess 1932-6203 PLoS ONE Engineering sciences. Technology info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion 2012 ftunivantwerpen https://doi.org/10.1371/JOURNAL.PONE.0044508 2023-06-26T22:16:31Z 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. Article in Journal/Newspaper Antarc* Antarctic Icefish IRUA - Institutional Repository van de Universiteit Antwerpen Antarctic The Antarctic PLoS ONE 7 12 e44508 |
institution |
Open Polar |
collection |
IRUA - Institutional Repository van de Universiteit Antwerpen |
op_collection_id |
ftunivantwerpen |
language |
English |
topic |
Engineering sciences. Technology |
spellingShingle |
Engineering sciences. Technology Giordano, Daniela Boron, Ignacio Abbruzzetti, Stefania Van Leuven, Wendy Moens, Luc Dewilde, Sylvia Biophysical characterisation of neuroglobin of the icefish, a natural knockout for hemoglobin and myoglobin : comparison with human neuroglobin |
topic_facet |
Engineering sciences. Technology |
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. |
format |
Article in Journal/Newspaper |
author |
Giordano, Daniela Boron, Ignacio Abbruzzetti, Stefania Van Leuven, Wendy Moens, Luc Dewilde, Sylvia |
author_facet |
Giordano, Daniela Boron, Ignacio Abbruzzetti, Stefania Van Leuven, Wendy Moens, Luc Dewilde, Sylvia |
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 |
publishDate |
2012 |
url |
https://hdl.handle.net/10067/1059730151162165141 https://repository.uantwerpen.be/docman/irua/686265/3910.pdf |
geographic |
Antarctic The Antarctic |
geographic_facet |
Antarctic The Antarctic |
genre |
Antarc* Antarctic Icefish |
genre_facet |
Antarc* Antarctic Icefish |
op_source |
1932-6203 PLoS ONE |
op_relation |
info:eu-repo/semantics/altIdentifier/doi/10.1371/JOURNAL.PONE.0044508 info:eu-repo/semantics/altIdentifier/isi/000312104700001 |
op_rights |
info:eu-repo/semantics/openAccess |
op_doi |
https://doi.org/10.1371/JOURNAL.PONE.0044508 |
container_title |
PLoS ONE |
container_volume |
7 |
container_issue |
12 |
container_start_page |
e44508 |
_version_ |
1771551073822048256 |