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...

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Published in:Molecular BioSystems
Main Authors: 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
Other Authors: 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
Language:English
Published: 2012
Subjects:
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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spelling 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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