ATP regulation of the ligand-binding properties in temperate and cold-adapted haemoglobins. X-ray structure and ligand-binding kinetics in the sub-Antarctic fish Eleginops maclovinus.
The major haemoglobin of the sub-Antarctic fish Eleginops maclovinus was structurally and functionally characterised with the aim to compare molecular environmental adaptations in the O2-transport system of sub-Antarctic fishes of the suborder Notothenioidei with those of their high-latitude relativ...
Published in: | Molecular BioSystems |
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2012
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Online Access: | http://hdl.handle.net/11588/512957 https://doi.org/10.1039/C2MB25210D http://pubs.rsc.org/en/Content/ArticleLanding/2012/MB/c2mb25210d |
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ftunivnapoliiris:oai:www.iris.unina.it:11588/512957 2024-09-09T19:03:45+00:00 ATP regulation of the ligand-binding properties in temperate and cold-adapted haemoglobins. X-ray structure and ligand-binding kinetics in the sub-Antarctic fish Eleginops maclovinus. D. Coppola S. Abbruzzetti F. Nicoletti A. Gambacurta D. Giordano B. D. Howes G. De Sanctis L. Vitagliano S. Bruno G. di Prisco L. Mazzarella G. Smulevich M. Coletta C. Viappiani C. Verde MERLINO, ANTONELLO VERGARA, ALESSANDRO D., Coppola S., Abbruzzetti F., Nicoletti Merlino, Antonello A., Gambacurta D., Giordano B. D., Howe G., De Sancti L., Vitagliano S., Bruno G., di Prisco L., Mazzarella G., Smulevich M., Coletta C., Viappiani Vergara, Alessandro C., Verde 2012 http://hdl.handle.net/11588/512957 https://doi.org/10.1039/C2MB25210D http://pubs.rsc.org/en/Content/ArticleLanding/2012/MB/c2mb25210d eng eng info:eu-repo/semantics/altIdentifier/wos/WOS:000311473200020 volume:8 issue:12 firstpage:3295 lastpage:3304 numberofpages:10 journal:MOLECULAR BIOSYSTEMS http://hdl.handle.net/11588/512957 doi:10.1039/C2MB25210D info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-84868138805 http://pubs.rsc.org/en/Content/ArticleLanding/2012/MB/c2mb25210d hemoglobin X-ray structure oxygen affinity Root-effect adaptation info:eu-repo/semantics/article 2012 ftunivnapoliiris https://doi.org/10.1039/C2MB25210D 2024-06-17T15:19:29Z The major haemoglobin of the sub-Antarctic fish Eleginops maclovinus was structurally and functionally characterised with the aim to compare molecular environmental adaptations in the O2-transport system of sub-Antarctic fishes of the suborder Notothenioidei with those of their high-latitude relatives. Ligand-binding kinetics of the major haemoglobin of E. maclovinus indicated strong stabilisation of the liganded quaternary T state, enhanced in the presence of the physiological allosteric effector ATP, compared to that of high-Antarctic Trematomus bernacchii. The activation enthalpy for O2 dissociation was dramatically lower than that in T. bernacchii haemoglobin, suggesting remarkable differences in temperature sensitivity and structural changes associated with O2 release and exit from the protein. The haemoglobin functional properties, together with the X-ray structure of the CO form at 1.49 Å resolution, the first of a temperate notothenioid, strongly support the hypothesis that in E. maclovinus, whose life-style varies according to changes in habitat, the mechanisms that regulate O2 affinity and the ATP-induced Root effect differ from those of high-Antarctic Notothenioids. Article in Journal/Newspaper Antarc* Antarctic IRIS Università degli Studi di Napoli Federico II Antarctic Molecular BioSystems 8 12 3295 |
institution |
Open Polar |
collection |
IRIS Università degli Studi di Napoli Federico II |
op_collection_id |
ftunivnapoliiris |
language |
English |
topic |
hemoglobin X-ray structure oxygen affinity Root-effect adaptation |
spellingShingle |
hemoglobin X-ray structure oxygen affinity Root-effect adaptation D. Coppola S. Abbruzzetti F. Nicoletti A. Gambacurta D. Giordano B. D. Howes G. De Sanctis L. Vitagliano S. Bruno G. di Prisco L. Mazzarella G. Smulevich M. Coletta C. Viappiani C. Verde MERLINO, ANTONELLO VERGARA, ALESSANDRO ATP regulation of the ligand-binding properties in temperate and cold-adapted haemoglobins. X-ray structure and ligand-binding kinetics in the sub-Antarctic fish Eleginops maclovinus. |
topic_facet |
hemoglobin X-ray structure oxygen affinity Root-effect adaptation |
description |
The major haemoglobin of the sub-Antarctic fish Eleginops maclovinus was structurally and functionally characterised with the aim to compare molecular environmental adaptations in the O2-transport system of sub-Antarctic fishes of the suborder Notothenioidei with those of their high-latitude relatives. Ligand-binding kinetics of the major haemoglobin of E. maclovinus indicated strong stabilisation of the liganded quaternary T state, enhanced in the presence of the physiological allosteric effector ATP, compared to that of high-Antarctic Trematomus bernacchii. The activation enthalpy for O2 dissociation was dramatically lower than that in T. bernacchii haemoglobin, suggesting remarkable differences in temperature sensitivity and structural changes associated with O2 release and exit from the protein. The haemoglobin functional properties, together with the X-ray structure of the CO form at 1.49 Å resolution, the first of a temperate notothenioid, strongly support the hypothesis that in E. maclovinus, whose life-style varies according to changes in habitat, the mechanisms that regulate O2 affinity and the ATP-induced Root effect differ from those of high-Antarctic Notothenioids. |
author2 |
D., Coppola S., Abbruzzetti F., Nicoletti Merlino, Antonello A., Gambacurta D., Giordano B. D., Howe G., De Sancti L., Vitagliano S., Bruno G., di Prisco L., Mazzarella G., Smulevich M., Coletta C., Viappiani Vergara, Alessandro C., Verde |
format |
Article in Journal/Newspaper |
author |
D. Coppola S. Abbruzzetti F. Nicoletti A. Gambacurta D. Giordano B. D. Howes G. De Sanctis L. Vitagliano S. Bruno G. di Prisco L. Mazzarella G. Smulevich M. Coletta C. Viappiani C. Verde MERLINO, ANTONELLO VERGARA, ALESSANDRO |
author_facet |
D. Coppola S. Abbruzzetti F. Nicoletti A. Gambacurta D. Giordano B. D. Howes G. De Sanctis L. Vitagliano S. Bruno G. di Prisco L. Mazzarella G. Smulevich M. Coletta C. Viappiani C. Verde MERLINO, ANTONELLO VERGARA, ALESSANDRO |
author_sort |
D. Coppola |
title |
ATP regulation of the ligand-binding properties in temperate and cold-adapted haemoglobins. X-ray structure and ligand-binding kinetics in the sub-Antarctic fish Eleginops maclovinus. |
title_short |
ATP regulation of the ligand-binding properties in temperate and cold-adapted haemoglobins. X-ray structure and ligand-binding kinetics in the sub-Antarctic fish Eleginops maclovinus. |
title_full |
ATP regulation of the ligand-binding properties in temperate and cold-adapted haemoglobins. X-ray structure and ligand-binding kinetics in the sub-Antarctic fish Eleginops maclovinus. |
title_fullStr |
ATP regulation of the ligand-binding properties in temperate and cold-adapted haemoglobins. X-ray structure and ligand-binding kinetics in the sub-Antarctic fish Eleginops maclovinus. |
title_full_unstemmed |
ATP regulation of the ligand-binding properties in temperate and cold-adapted haemoglobins. X-ray structure and ligand-binding kinetics in the sub-Antarctic fish Eleginops maclovinus. |
title_sort |
atp regulation of the ligand-binding properties in temperate and cold-adapted haemoglobins. x-ray structure and ligand-binding kinetics in the sub-antarctic fish eleginops maclovinus. |
publishDate |
2012 |
url |
http://hdl.handle.net/11588/512957 https://doi.org/10.1039/C2MB25210D http://pubs.rsc.org/en/Content/ArticleLanding/2012/MB/c2mb25210d |
geographic |
Antarctic |
geographic_facet |
Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_relation |
info:eu-repo/semantics/altIdentifier/wos/WOS:000311473200020 volume:8 issue:12 firstpage:3295 lastpage:3304 numberofpages:10 journal:MOLECULAR BIOSYSTEMS http://hdl.handle.net/11588/512957 doi:10.1039/C2MB25210D info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-84868138805 http://pubs.rsc.org/en/Content/ArticleLanding/2012/MB/c2mb25210d |
op_doi |
https://doi.org/10.1039/C2MB25210D |
container_title |
Molecular BioSystems |
container_volume |
8 |
container_issue |
12 |
container_start_page |
3295 |
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1809817781569323008 |