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Asymmetric hemoglobin hybrids

M C Marden1, N Griffon, C Poyart

  • 1INSERM U299, Hôpital de Bicêtre, Le Kremlin Bicêtre, France.

Journal of Molecular Biology
|October 18, 1996
PubMed
Summary
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Hemoglobin valency hybrids' functional properties were studied. The position of oxidized subunits did not affect CO recombination kinetics, suggesting a kinetic factor influences allosteric equilibrium.

Area of Science:

  • Biochemistry
  • Biophysics

Background:

  • Hemoglobin (Hb) exhibits complex allosteric regulation.
  • Valency hybrids of Hb, with varying oxidation states, offer insights into these mechanisms.

Purpose of the Study:

  • To investigate the functional properties of hemoglobin valency hybrids.
  • To determine if the arrangement of oxidized subunits (asymmetric vs. symmetric) influences allosteric equilibrium.

Main Methods:

  • Preparation of asymmetric Hb valency hybrids by mixing HbCO and cyano-metHb.
  • Flash photolysis to study CO recombination kinetics.
  • Analysis of allosteric equilibrium using CO rebinding rates.

Main Results:

  • Mixing HbCO with cyano-metHb reduced the slow phase of CO recombination, indicating a shift from the T-state.

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  • The ratio of HbCN to HbCO influenced the observed slow fraction.
  • No significant difference was observed between asymmetric and symmetric hybrids, contrary to expectations.

    • Conclusions:

    • The arrangement of oxidized subunits in Hb valency hybrids does not appear to significantly alter CO recombination kinetics.
    • Observed discrepancies with prior equilibrium studies may be attributed to kinetic factors, such as slow relaxation to the T-state post-photolysis.