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Functional differentiation in trematode hemoglobin isoforms.

A K Rashid1, R E Weber

  • 1Danish Center for Respiratory Adaptation (CRA), Department of Zoophysiology, Institute of Biological Sciences, Denmark.

European Journal of Biochemistry
|April 2, 1999
PubMed
Summary
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Trematode hemoglobins (Hbs) bind O2 and CO with exceptionally high affinity, up to 800 times greater than human Hbs. Unique Tyr substitutions in these parasitic worms

Area of Science:

  • Biochemistry
  • Parasitology
  • Structural Biology

Background:

  • Hemoglobins (Hbs) in parasitic trematodes, such as Explanatum explanatum, Gastrothylax crumenifer, and Paramphistomum epiclitum, are crucial for oxygen transport.
  • These trematodes parasitize the common Indian water buffalo Bubalus bubalis, making their Hbs relevant to host-parasite interactions.

Purpose of the Study:

  • To isolate and characterize hemoglobins (Hbs) and their isoforms from three trematode species.
  • To investigate the oxygen (O2) binding properties and affinities of these trematode Hbs.
  • To elucidate the structural basis for the unique O2 binding characteristics.

Main Methods:

  • Isolation of Hbs and isoHbs via electrophoresis from three trematode species.
  • O2 equilibrium studies to determine O2 affinities and half-saturation O2 tension (P50) values.

Related Experiment Videos

  • Analysis of structural features, including Tyr residue substitutions at B10 and E7 positions, and their impact on O2 binding kinetics and autoxidation.

    • Main Results:

    • Trematode Hbs are monomeric and possess extremely high O2 affinities (P50 values up to 800 times lower than human Hbs).
    • High O2 affinity is attributed to Tyr residues at B10 and E7, which form hydrogen bonds with O2 and hinder water entry into the heme pocket.
    • CO binding is less competitive than O2 binding, with partition coefficients (M) below 1, contrasting with vertebrate Hbs.

    Conclusions:

    • Trematode Hbs exhibit unique, highly efficient O2 binding mechanisms due to specific amino acid substitutions.
    • These adaptations are crucial for survival in low-oxygen environments associated with parasitic infections.
    • The findings provide insights into the functional diversity of hemoglobins across different species.