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Related Experiment Videos

Structural basis for the root effect in haemoglobin

S E Mylvaganam1, C Bonaventura, J Bonaventura

  • 1The Scripps Research Institute, La Jolla, California 92037, USA.

Nature Structural Biology
|March 1, 1996
PubMed
Summary
This summary is machine-generated.

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Root effect hemoglobins achieve high oxygen transport by drastically lowering oxygen affinity at acidic pH. A crystal structure reveals key residues destabilize the R-state, triggering oxygen release.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Physiology

Background:

  • Root effect hemoglobins exhibit unique oxygen transport properties, enabling oxygen pumping against high gradients.
  • These properties are linked to extreme reductions in oxygen affinity and cooperativity under acidic conditions.

Purpose of the Study:

  • To elucidate the molecular mechanism underlying the root effect in hemoglobin.
  • To investigate the structural basis for acid-induced oxygen release.

Main Methods:

  • X-ray crystallography to determine the 2 angstrom crystal structure of ligand-bound hemoglobin from Leiostomus xanthurus at pH 7.5.

Main Results:

  • The structure reveals that the root effect involves modulation of the R-state (high-affinity state).

Related Experiment Videos

  • Positive-charge clusters at the allosteric beta1-beta2 interface in the R-state are formed by key residues.
  • Protonation of specific residues at low pH destabilizes the R-state, promoting an R to T state transition and oxygen release.
  • Unique residues in root effect hemoglobins recruit conserved residues to generate the root effect.

    • Conclusions:

    • The root effect mechanism involves acid-induced destabilization of the R-state through specific residue protonation.
    • Structural insights explain how root effect hemoglobins achieve their specialized oxygen transport function.