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 O-2-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 O-2 dissociation was dramatically lower than that in T. bernacchii haemoglobin, suggesting remarkable differences in temperature sensitivity and structural changes associated with O-2 release and exit from the protein. The haemoglobin functional properties, together with the X-ray structure of the CO form at 1.49 angstrom 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 O-2 affinity and the ATP-induced Root effect differ from those of high-Antarctic Notothenioids.

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 / Daniela Coppola; Stefania Abbruzzetti; Francesco Nicoletti; Antonello Merlinod; Alessandra Gambacurta; Daniela Giordano; Barry D. Howes; Giampiero De Sanctis; Luigi Vitagliano; Stefano Bruno; Guido di Prisco; Lelio Mazzarella; Giulietta Smulevich; Massimo Coletta; Cristiano Viappiani; Alessandro Vergara; Cinzia Verde. - In: MOLECULAR BIOSYSTEMS. - ISSN 1742-206X. - STAMPA. - 12:(2012), pp. 3295-3304. [10.1039/c2mb25210d]

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

HOWES, BARRY DENNIS;SMULEVICH, GIULIETTA;
2012

Abstract

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 O-2-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 O-2 dissociation was dramatically lower than that in T. bernacchii haemoglobin, suggesting remarkable differences in temperature sensitivity and structural changes associated with O-2 release and exit from the protein. The haemoglobin functional properties, together with the X-ray structure of the CO form at 1.49 angstrom 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 O-2 affinity and the ATP-induced Root effect differ from those of high-Antarctic Notothenioids.
2012
12
3295
3304
Daniela Coppola; Stefania Abbruzzetti; Francesco Nicoletti; Antonello Merlinod; Alessandra Gambacurta; Daniela Giordano; Barry D. Howes; Giampiero De ...espandi
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Utilizza questo identificatore per citare o creare un link a questa risorsa: https://hdl.handle.net/2158/822411
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