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 (669 views)
Molecular Biosystems (ISSN: 1742-206x), 2012 Oct 30; 8(12): 3295-3304.
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Paper type: Journal Article,
Impact factor: 3.35, 5-year impact factor: 3.575
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84868138805&partnerID=40&md5=499a94c7fdc2477fd40bb6075be3fe6f
Keywords: Eleginops Maclovinus, Notothenioidei, Pisces, Trematomus Bernacchii, Adenosine Triphosphate, Carbon Monoxide, Carboxyhemoglobin, Ligand, Oxygen, Adaptation, Animal, Antarctica, Article, Chemistry, Cold, Dna Sequence, Ecosystem, Genetics, Kinetics, Metabolism, Oxygen Consumption, Perciformes, Phylogeny, Thermodynamics, X Ray Crystallography, Physiological, Antarctic Regions, Cold Temperature, X-Ray, Sequence Analysis,
Affiliations:
*** IBB - CNR ***
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
References:
Not available.
Molecular Biosystems (ISSN: 1742-206x), 2012 Oct 30; 8(12): 3295-3304.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 3.35, 5-year impact factor: 3.575
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84868138805&partnerID=40&md5=499a94c7fdc2477fd40bb6075be3fe6f
Keywords: Eleginops Maclovinus, Notothenioidei, Pisces, Trematomus Bernacchii, Adenosine Triphosphate, Carbon Monoxide, Carboxyhemoglobin, Ligand, Oxygen, Adaptation, Animal, Antarctica, Article, Chemistry, Cold, Dna Sequence, Ecosystem, Genetics, Kinetics, Metabolism, Oxygen Consumption, Perciformes, Phylogeny, Thermodynamics, X Ray Crystallography, Physiological, Antarctic Regions, Cold Temperature, X-Ray, Sequence Analysis,
Affiliations:
*** IBB - CNR ***
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
References:
Not available.
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.
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
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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
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View Export to BibTeX Export to EndNote
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Vitagliano L, Vergara A, Bonomi G, Merlino A, Verde C, Di Prisco G, Howes BD, Smulevich G, Mazzarella L
* Spectroscopic and crystallographic characterization of a tetrameric hemoglobin oxidation reveals structural features of the functional intermediate relaxed/tense state (938 views)
J Am Chem Soc (ISSN: 0002-7863, 0002-2786, 1520-5126), 2008 Sep 13; 130(32): 10527-10535.
Impact Factor: 8.091
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Sinibaldi F, Fiorucci L, Patriarca A, Lauceri R, Ferri T, Coletta M, Santucci R
* Insights into cytochrome c-cardiolipin interaction. Role played by ionic strength (785 views)
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 2008 Jul 1; 47(26): 6928-6935.
Impact Factor: 3.379
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Atlante A, Amadoro G, Bobba A, de Bari L, Corsetti V, Pappalardo G, Marra E, Calissano P, Passarella S
* A peptide containing residues 26-44 of tau protein impairs mitochondrial oxidative phosphorylation acting at the level of the adenine nucleotide translocator (941 views)
Bba-Gen Subjects (ISSN: 0005-2728, 0006-3002print, 0006-3002linking), 2008; 1777(10): 1289-1300.
Impact Factor: 4.447
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Merlino A, Verde C, Di Prisco G, Mazzarella L, Vergara A
* Reduction of ferric hemoglobin from Trematomus bernacchii in a partial bis-histidyl state produces a deoxy coordination even when encapsulated into the crystal phase (738 views)
Spectroscopy An International Journal (ISSN: 0712-4813), 2008; 22(2-3): 143-152.
Impact Factor: 0.82
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Giordano D, Vergara A, Lee HC, Peisach J, Balestrieri M, Mazzarella L, Parisi E, Di Priseo G, Verde C
* Hemoglobin structure/function and globin-gene evolution in the Arctic fish Liparis tunicatus (1596 views)
Gene (ISSN: 0378-1119), 2007 Dec 30; 406(1-2): 58-68.
Impact Factor: 2.871
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Vergara A, Franzese M, Merlino A, Vitagliano L, Verde C, Di Prisco G, Lee HC, Peisach J, Mazzarella L
* Structural characterization of ferric hemoglobins from three Antarctic fish species of the suborder notothenioidei (714 views)
Biophysical Journal (ISSN: 0006-3495, 1542-0086), 2007 Oct; 93(8): 2822-2829.
Impact Factor: 4.627
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Papa S, Monti SM, Vitale RM, Bubici C, Jayawardena S, Alvarez K, De Smaele E, Dathan N, Pedone C, Ruvo M, Franzoso G
* Insights Into The Structural Basis Of The Gadd45beta-Mediated Inactivation Of The Jnk Kinase, Mkk7/Jnkk2 (1053 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2007 Jun 29; 282(26): 19029-19041.
Impact Factor: 5.581
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Mazzarella L, Vergara A, Vitagliano L, Merlino A, Bonomi G, Scala S, Verde C, Di Prisco G
* High resolution crystal structure of deoxy hemoglobin from Trematomus bernacchii at different pH values: The role of histidine residues in modulating the strength of the root effect (620 views)
Proteins (ISSN: 0887-3585, 1097-0134, 1097-0134electronic), 2006 Nov 1; 65(2): 490-498.
Impact Factor: 3.73
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Pedone E, Bartolucci S, Fiorentino G
* Sensing and adapting to environmental stress: The Archaeal tactic (592 views)
Frontiers In Bioscience (ISSN: 1093-9946, 1093-4715), 2004 Sep 1; 9: 2909-2926.
Impact Factor: 3.226
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Vitagliano L, Bonomi G, Riccio A, di Prisco G, Smulevich G, Mazzarella L
* The oxidation process of Antarctic fish hemoglobins (729 views)
Eur J Biochem (ISSN: 0014-2956, 0014-2956print), 2004 May; 271(9): 1651-1659.
Impact Factor: 3.26
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Clemente F, D'Avino E, Guaragno M, Menichetti A
* An on line technique to detect cardiac output variations and cardiovascular performances during abdominal aortic surgery (923 views)
Journal Of Clinical Monitoring And Computing (ISSN: 1387-1307), 2004 Apr; 18(2): 81-87.
Impact Factor: 0.888
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Riccio A, Vitagliano L, Di Prisco G, Zagari A, Mazzarella L
* Liganded and unliganded forms of Antarctic fish haemoglobins in polyethylene glycol: crystallization of an R-state haemichrome intermediate (699 views)
Acta Crystallogr D Biol Crystallogr (ISSN: 0907-4449, 0907-4449linking), 2001 Sep; 57: 1144-1146.
Impact Factor: 2.124
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Aime S, Dastrù W, Gobetto R, Viale A
An NMR study of H(μ-H)Os3(CO)11 (619 views)
Inorg Chem (ISSN: 0020-1669, 1520-510x, 1520-510xelectronic), 2000; 39(11): 2422-2425.
Impact Factor: 2.712
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Del Vecchio S, Ciarmiello A, Salvatore M
Clinical imaging of multidrug resistance in cancer (675 views)
Q J Nucl Med (ISSN: 1124-3937, 1125-0135), 1999 Jun; 43(2): 125-131.
Impact Factor: 2.125
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FRITTITTA L, VIGNERI R, PAPA V, GOLDFINE I, GRASSO G, TRISCHITTA V
Structural and functional studies of insulin receptors in human breast cancer (660 views)
Breast Cancer Res Tr Kluwer Academic Publishers (ISSN: 0167-6806), 1993; 25(1): 73-82.
Impact Factor: 2.43
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Romano M, Cerra M, Salvatore M, Onorati A
Effects of ionizing radiations on the activity of valyl tRNA synthetase isolated from rat liver and from Morris hepatoma 7777 (1235 views)
Tumori (ISSN: 0300-8916, 0300-8916print, 0300-8916linking), 1974 Jul; 60(4): 301-306.
Impact Factor: 0.408
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32 Records (32 excluding Abstracts).
Total impact factor: 136.816 (136.816 excluding Abstracts).
Total 5 year impact factor: 154.76 (154.76 excluding Abstracts).
Total impact factor: 136.816 (136.816 excluding Abstracts).
Total 5 year impact factor: 154.76 (154.76 excluding Abstracts).
669 views. Last view on Thursday 17 April 2025, 15:41:47
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