4.0 Article

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

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INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S1744309110038698

Keywords

cold adaptation; Eleginops maclovinus; haemichrome; haemoglobin; oxygen affinity; Raman microspectroscopy

Funding

  1. PNRA (Italian National Programme for Antarctic Research)
  2. Scientific Committee for Antarctic Research (SCAR)
  3. Ministero Italiano dell'Universita e della Ricerca Scientifica [PRIN 2007SFZXZ7]
  4. National Science Foundation [OPP 0132032]

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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.

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