1. Crystallization, preliminary X-ray diffraction studies and Raman microscopy of the major haemoglobin from the sub-Antarctic fishEleginops maclovinusin the carbomonoxy form
- Author
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Luigi Vitagliano, Daniela Giordano, Anna Balsamo, Daniela Coppola, Giulietta Smulevich, Francesco P. Nicoletti, Antonello Merlino, Barry D. Howes, Lelio Mazzarella, Guido di Prisco, Alessandro Vergara, Cinzia Verde, Merlino, Antonello, Vitagliano, L, Balsamo, A, Nicoletti, Fp, Howes, Bd, Giordano, D, Coppola, D, di Prisco, G, Verde, C, Smulevich, G, Mazzarella, Lelio, and Vergara, Alessandro
- Subjects
raman ,Biophysics ,Analytical chemistry ,Crystallography, X-Ray ,Spectrum Analysis, Raman ,Biochemistry ,law.invention ,Crystal ,symbols.namesake ,Structural Biology ,law ,Genetics ,Animals ,Crystallization ,crystallography ,biology ,Chemistry ,Root effect ,Eleginops maclovinus ,hemoglobin ,Condensed Matter Physics ,HEXA ,biology.organism_classification ,Perciformes ,Crystallography ,Carboxyhemoglobin ,Crystallization Communications ,X-ray crystallography ,symbols ,Orthorhombic crystal system ,Raman spectroscopy - 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.
- Published
- 2010
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