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Related Experiment Videos

Trematode hemoglobins show exceptionally high oxygen affinity

L Kiger1, A K Rashid, N Griffon

  • 1INSERM U473, 94276 Le Kremlin Bicêtre Cedex, France.

Biophysical Journal
|July 24, 1998
PubMed
Summary

Trematode hemoglobins exhibit exceptionally high oxygen affinity due to fast binding and slow release kinetics. These parasitic worms possess unique structural features, including tyrosine residues, contributing to their remarkable oxygen-binding capabilities.

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Area of Science:

  • Biochemistry
  • Parasitology
  • Structural Biology

Background:

  • Hemoglobin (Hb) function is critical for oxygen transport in diverse organisms.
  • Parasitic trematodes living in aquatic environments require efficient oxygen uptake and utilization.
  • Comparative studies of hemoglobin structure-function relationships provide insights into evolutionary adaptations.

Purpose of the Study:

  • To investigate the ligand binding kinetics and structural properties of hemoglobins from various trematode species.
  • To compare the oxygen and carbon monoxide binding characteristics of trematode hemoglobins with other known hemoglobins.
  • To elucidate the molecular basis for the observed high oxygen affinity in trematode hemoglobins.

Main Methods:

  • Isolation and purification of hemoglobins from Gastrothylax crumenifer (Gc), Paramphistomum epiclitum (Pe), Explanatum explanatum (Ee), and Isoparorchis hypselobagri (Ih).

Related Experiment Videos

  • Kinetic studies of oxygen and carbon monoxide binding and dissociation using spectroscopy.
  • Analysis of autoxidation rates and reactivity with oxidizing agents.
  • Amino acid sequence analysis focusing on key residue positions (e.g., E7, B10).

    • Main Results:

    • Trematode hemoglobins display very fast association rates for oxygen and carbon monoxide.
    • Oxygen dissociation from trematode hemoglobins is significantly slower (seconds to >20s) compared to human Hb (milliseconds).
    • Carbon monoxide dissociation is faster than in other monomeric hemoglobins or myoglobins.
    • Reduced autoxidation rates were observed, with only the deoxy form reacting rapidly with potassium ferricyanide.
    • Unique structural features, including tyrosine at position E7 and B10, are present, potentially forming two hydrogen bonds to the oxygen molecule.
    • These factors contribute to some of the highest oxygen affinities ever recorded.

    Conclusions:

    • Trematode hemoglobins possess exceptionally high oxygen affinities, surpassing many known hemoglobins.
    • The combination of rapid ligand association and extremely slow dissociation rates is key to their high oxygen affinity.
    • Structural adaptations, particularly the presence of tyrosine residues at specific positions, are responsible for the enhanced oxygen binding.
    • These findings highlight specialized adaptations of hemoglobin in parasitic organisms for efficient oxygen management in their specific environments.