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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Online Access: | http://hdl.handle.net/11381/2451236 https://doi.org/10.1371/journal.pone.0044508 |
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ftunivparmairis:oai:air.unipr.it:11381/2451236 2024-04-21T07:46:46+00:00 Biophysical characterisation of neuroglobin of the icefish, a natural knockout for hemoglobin and myoglobin. Comparison with human neuroglobin D. Giordano I. Boron W. Van Leuven F. Nicoletti F. Forti C. H. C. Cheng L. Moens G. di Prisco A. Nadra D. Estrin G. Smulevich S. Dewilde C. Verde ABBRUZZETTI, Stefania BRUNO, Stefano VIAPPIANI, Cristiano D., Giordano I., Boron Abbruzzetti, Stefania W., Van Leuven F., Nicoletti F., Forti Bruno, Stefano C. H. C., Cheng L., Moen G., di Prisco A., Nadra D., Estrin G., Smulevich S., Dewilde Viappiani, Cristiano C., Verde 2012 http://hdl.handle.net/11381/2451236 https://doi.org/10.1371/journal.pone.0044508 eng eng info:eu-repo/semantics/altIdentifier/wos/WOS:000312104700001 volume:7 issue:12 firstpage:e44508 numberofpages:11 journal:PLOS ONE http://hdl.handle.net/11381/2451236 doi:10.1371/journal.pone.0044508 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-84870693871 info:eu-repo/semantics/article 2012 ftunivparmairis https://doi.org/10.1371/journal.pone.0044508 2024-03-28T01:17:50Z 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, the Antarctic fish neuroglobins can reversibly bind oxygen and CO in the Fe2+ form, and show six-coordinatio 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 Archivio della ricerca dell'Università di Parma (CINECA IRIS) PLoS ONE 7 12 e44508 |
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Archivio della ricerca dell'Università di Parma (CINECA IRIS) |
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ftunivparmairis |
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, the Antarctic fish neuroglobins can reversibly bind oxygen and CO in the Fe2+ form, and show six-coordinatio 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. |
author2 |
D., Giordano I., Boron Abbruzzetti, Stefania W., Van Leuven F., Nicoletti F., Forti Bruno, Stefano C. H. C., Cheng L., Moen G., di Prisco A., Nadra D., Estrin G., Smulevich S., Dewilde Viappiani, Cristiano C., Verde |
format |
Article in Journal/Newspaper |
author |
D. Giordano I. Boron W. Van Leuven F. Nicoletti F. Forti C. H. C. Cheng L. Moens G. di Prisco A. Nadra D. Estrin G. Smulevich S. Dewilde C. Verde ABBRUZZETTI, Stefania BRUNO, Stefano VIAPPIANI, Cristiano |
spellingShingle |
D. Giordano I. Boron W. Van Leuven F. Nicoletti F. Forti C. H. C. Cheng L. Moens G. di Prisco A. Nadra D. Estrin G. Smulevich S. Dewilde C. Verde ABBRUZZETTI, Stefania BRUNO, Stefano VIAPPIANI, Cristiano Biophysical characterisation of neuroglobin of the icefish, a natural knockout for hemoglobin and myoglobin. Comparison with human neuroglobin |
author_facet |
D. Giordano I. Boron W. Van Leuven F. Nicoletti F. Forti C. H. C. Cheng L. Moens G. di Prisco A. Nadra D. Estrin G. Smulevich S. Dewilde C. Verde ABBRUZZETTI, Stefania BRUNO, Stefano VIAPPIANI, Cristiano |
author_sort |
D. Giordano |
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/11381/2451236 https://doi.org/10.1371/journal.pone.0044508 |
genre |
Antarc* Antarctic Icefish |
genre_facet |
Antarc* Antarctic Icefish |
op_relation |
info:eu-repo/semantics/altIdentifier/wos/WOS:000312104700001 volume:7 issue:12 firstpage:e44508 numberofpages:11 journal:PLOS ONE http://hdl.handle.net/11381/2451236 doi:10.1371/journal.pone.0044508 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-84870693871 |
op_doi |
https://doi.org/10.1371/journal.pone.0044508 |
container_title |
PLoS ONE |
container_volume |
7 |
container_issue |
12 |
container_start_page |
e44508 |
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1796944517339807744 |