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Related Experiment Videos

Hagfish hemoglobins: structure, function, and oxygen-linked association.

A Fago1, L Giangiacomo, R D'Avino

  • 1Department of Zoophysiology, University of Aarhus, Bldg. 131, Universitetsparken, DK 8000 Aarhus C, Denmark.

The Journal of Biological Chemistry
|April 11, 2001
PubMed
Summary

Hagfish hemoglobins HbI, HbII, and HbIII exhibit distinct polymerization and pH-dependent oxygen binding behaviors, with HbII forming dimers and showing a Bohr effect, unlike HbI and HbIII.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Evolutionary Biology

Background:

  • Cyclostomes, including hagfish and lampreys, possess unique hemoglobins that polymerize upon deoxygenation.
  • The hemoglobin structure and function in these primitive vertebrates offer insights into protein evolution and oxygen transport.

Purpose of the Study:

  • To characterize the three major hemoglobin components (HbI, HbII, HbIII) from the hagfish Myxine glutinosa.
  • To compare these hagfish hemoglobins with the known structure of lamprey Petromyzon marinus HbV.
  • To investigate the functional implications of structural differences, including polymerization, pH dependence, and heteropolymer formation.

Main Methods:

  • Ultracentrifugation to determine hemoglobin quaternary structure under varying conditions.

Related Experiment Videos

  • Infrared spectroscopy to probe the distal pocket and CO binding kinetics.
  • Comparative sequence analysis and functional assays (oxygen affinity, Bohr effect).

    • Main Results:

    • HbI and HbIII from M. glutinosa are monomeric and pH-independent, with substitutions at the distal histidine and deoxy dimer interface.
    • HbII exhibits sequence similarity to P. marinus HbV, forms dimers at acidic pH, and displays a Bohr effect.
    • HbII can form functional heterodimers and heterotetramers with HbI and HbIII, exhibiting cooperativity and linked proton/bicarbonate binding.

    Conclusions:

    • Hagfish hemoglobins display diverse functional properties, reflecting adaptations in oxygen transport.
    • Structural variations, particularly in the distal pocket and dimer interface, correlate with observed functional differences.
    • The capacity for heteropolymer formation in hagfish hemoglobins suggests complex regulatory mechanisms for oxygen delivery.