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Naoya Shibayama1, Kanako Sugiyama, Jeremy R H Tame

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Human hemoglobin exhibits multiple intermediate states between its tense (T) and relaxed (R) forms. This study captures nine distinct conformers, revealing a previously unknown intermediate with unique oxygen affinity.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Protein Dynamics

Background:

  • Allostery in oligomeric proteins is often modeled as a transition between tense (T) and relaxed (R) states.
  • Hemoglobin (Hb) structure-function relationships are extensively studied, but intermediate states remain poorly understood.
  • Dynamic equilibrium of intermediate conformers hinders conventional characterization.

Purpose of the Study:

  • To structurally and functionally characterize multiple equilibrium conformers of human hemoglobin.
  • To elucidate the complete conformational space and transition pathway of hemoglobin.
  • To identify novel intermediate states and their properties.

Main Methods:

  • Combined X-ray diffraction analysis and microspectrophotometric O2 equilibrium measurements.
  • Utilized three isomorphous crystals, each capturing three distinct equilibrium conformers.
  • Analyzed nine complete structural and functional snapshots of hemoglobin conformers.

Main Results:

  • Captured nine distinct equilibrium conformers of human hemoglobin, spanning the T to R2 conformational range.
  • Identified various relaxed intermediate forms between R and R2 states.
  • Discovered a novel intermediate conformer between T and R states with intermediate O2 affinity.

Conclusions:

  • Human hemoglobin exists in a dynamic equilibrium of multiple conformers, not just discrete T and R states.
  • The identified conformers provide a comprehensive view of the hemoglobin transition pathway.
  • The novel T-R intermediate offers insights into oxygen binding regulation.