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...
Published in: | PLoS ONE |
---|---|
Main Authors: | , , , , , , , , , , , , , , , |
Format: | Article in Journal/Newspaper |
Language: | English |
Published: |
2012
|
Subjects: | |
Online Access: | https://www.vliz.be/imisdocs/publications/295994.pdf |
id |
ftvliz:oai:oma.vliz.be:280698 |
---|---|
record_format |
openpolar |
spelling |
ftvliz:oai:oma.vliz.be:280698 2023-05-15T13:54:11+02:00 Biophysical characterisation of neuroglobin of the icefish, a natural knockout for hemoglobin and myoglobin. Comparison with human neuroglobin 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 application/pdf https://www.vliz.be/imisdocs/publications/295994.pdf en eng info:eu-repo/semantics/altIdentifier/wos/000312104700001 info:eu-repo/semantics/altIdentifier/doi/doi.org/10.1371/journal.pone.0044508 https://www.vliz.be/imisdocs/publications/295994.pdf info:eu-repo/semantics/openAccess %3Ci%3EPLoS+One+7%2812%29%3C%2Fi%3E%3A+e44508.+%3Ca+href%3D%22https%3A%2F%2Fdx.doi.org%2F10.1371%2Fjournal.pone.0044508%22+target%3D%22_blank%22%3Ehttps%3A%2F%2Fdx.doi.org%2F10.1371%2Fjournal.pone.0044508%3C%2Fa%3E info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion 2012 ftvliz https://doi.org/10.1371/journal.pone.0044508 2022-05-01T10:44:45Z 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. Article in Journal/Newspaper Antarc* Antarctic Icefish Flanders Marine Institute (VLIZ): Open Marine Archive (OMA) Antarctic The Antarctic PLoS ONE 7 12 e44508 |
institution |
Open Polar |
collection |
Flanders Marine Institute (VLIZ): Open Marine Archive (OMA) |
op_collection_id |
ftvliz |
language |
English |
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. |
format |
Article in Journal/Newspaper |
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. |
spellingShingle |
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 |
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 |
https://www.vliz.be/imisdocs/publications/295994.pdf |
geographic |
Antarctic The Antarctic |
geographic_facet |
Antarctic The Antarctic |
genre |
Antarc* Antarctic Icefish |
genre_facet |
Antarc* Antarctic Icefish |
op_source |
%3Ci%3EPLoS+One+7%2812%29%3C%2Fi%3E%3A+e44508.+%3Ca+href%3D%22https%3A%2F%2Fdx.doi.org%2F10.1371%2Fjournal.pone.0044508%22+target%3D%22_blank%22%3Ehttps%3A%2F%2Fdx.doi.org%2F10.1371%2Fjournal.pone.0044508%3C%2Fa%3E |
op_relation |
info:eu-repo/semantics/altIdentifier/wos/000312104700001 info:eu-repo/semantics/altIdentifier/doi/doi.org/10.1371/journal.pone.0044508 https://www.vliz.be/imisdocs/publications/295994.pdf |
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_ |
1766259846521290752 |