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
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(343 views) Coppola D, Abbruzzetti S, Nicoletti F, Merlino A, Gambacurta A, Giordano D, Howes BD, De Sanctis G, Vitagliano L, Bruno S, di Prisco G, Mazzarella L, Smulevich G, Coletta M, Viappiani C, Vergara A, Verde C
Molecular Biosystems (ISSN: 1742-206x), 2012 Oct 30; 8(12): 3295-3304.
Institute of Protein Biochemistry, CNR, Via Pietro Castellino 111, I-80131 Naples, Italy
Dipartimento di Fisica, Università Degli Studi di Parma, viale delle Scienze 7A, 43124 Parma, Italy
Istituto Nanoscienze, CNR, Piazza San Silvestro 12, 56127 Pisa, Italy
Dipartimento di Chimica ugo Schiff, Università di Firenze, Via della Lastruccia 3-13, 50019 Sesto Fiorentino (FI), Italy
Department of Chemical Sciences, University of Naples Federico II, Complesso Universitario Monte S. Angelo, Via Cinthia, 80126 Naples, Italy
Istituto di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 6, I-80134 Naples, Italy
Dipartimento di Medicina Sperimentale e Chirurgia, Università di Roma Tor Vergata, Via Montpellier 1, 00133 Roma, Italy
Scuola di Bioscienze e Biotecnologie, Università di Camerino, 62032 Camerino (MC), Italy
Dipartimento di Biochimica e Biologia Molecolare, Università di Parma, Viale G.P. Usberti 23/A, 43100 Parma, Italy
Department of Clinical Sciences and Translational Medicine, Università di Roma Tor, Vergata Via Montpellier 1, 00133 Rome, Italy
Interuniversity Consortium for the Research on the Chemistry of Metals in Biological Systems, Via C. Ulpiani 27, 70126 Bari, Italy
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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 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
No results.
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