The blood of the sub-Antarctic fish Eleginops maclovinus (Em) contains three haemoglobins. The major haemoglobin (Hb1Em) displays the Root effect, a drastic decrease in the oxygen affinity and a loss of cooperativity at acidic pH. The carbomonoxy form of HbEm1 has been crystallized in two different crystal forms, orthorhombic (Ortho) and hexagonal (Hexa), and high-resolution diffraction data have been collected for both forms (1.45 and 1.49 A ˚ resolution, respectively). The high-frequency resonance Raman spectra collected from the two crystal forms using excitation at 514 nm were almost indistinguishable. Hb1Em is the first sub-Antarctic fish Hb to be crystallized and its structural characterization will shed light on the molecular mechanisms of cold adaptation and the role of the Root effect in fish haemoglobins

Crystallization, preliminary X-ray diffraction studies and Raman microscopy of the major hemoglobin from the sub-Antarctic fish Eleginops maclovinus in the carbomonoxy form / A. Merlino; L. Vitagliano; A. Balsamo; F. Nicoletti; B. D. Howes; D. Giordano; D. Coppola; G. di Prisco; C. Verde; G. Smulevich; L. Mazzarella; A. Vergara. - In: ACTA CRYSTALLOGRAPHICA. SECTION F, STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS. - ISSN 1744-3091. - STAMPA. - F66:(2010), pp. 1536-1540. [10.1107/S1744309110038698]

Crystallization, preliminary X-ray diffraction studies and Raman microscopy of the major hemoglobin from the sub-Antarctic fish Eleginops maclovinus in the carbomonoxy form.

NICOLETTI, FRANCESCO PAOLO;HOWES, BARRY DENNIS;SMULEVICH, GIULIETTA;
2010

Abstract

The blood of the sub-Antarctic fish Eleginops maclovinus (Em) contains three haemoglobins. The major haemoglobin (Hb1Em) displays the Root effect, a drastic decrease in the oxygen affinity and a loss of cooperativity at acidic pH. The carbomonoxy form of HbEm1 has been crystallized in two different crystal forms, orthorhombic (Ortho) and hexagonal (Hexa), and high-resolution diffraction data have been collected for both forms (1.45 and 1.49 A ˚ resolution, respectively). The high-frequency resonance Raman spectra collected from the two crystal forms using excitation at 514 nm were almost indistinguishable. Hb1Em is the first sub-Antarctic fish Hb to be crystallized and its structural characterization will shed light on the molecular mechanisms of cold adaptation and the role of the Root effect in fish haemoglobins
2010
F66
1536
1540
A. Merlino; L. Vitagliano; A. Balsamo; F. Nicoletti; B. D. Howes; D. Giordano; D. Coppola; G. di Prisco; C. Verde; G. Smulevich; L. Mazzarella; A. Vergara
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Utilizza questo identificatore per citare o creare un link a questa risorsa: https://hdl.handle.net/2158/550271
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