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Updated: Jan 30 2017

Oxygen Transport and Hemoglobin

  • Hemoglobin
    • Forms of O2 in Blood
      • dissolved O2
        • 2% of total O2 content
      • O2 bound to hemoglobin
        • 98% of total O2 content
    • Hemoglobin
      • a globular protein conisisting of 4 polypeptide subunits
        • 2 α subunits and 2 β subunits
        • binds 4 O2 molecules
          • each subunit contains a heme moiety (iron-binding porphyrin ring)
            • iron in heme moieties is in reduced, ferrous state (Fe2+)
              • Fe2+ binds O2 reversibly
      • exists in 2 states
        • low O2 affinity T (taut) state
        • high O2 affinity R (relaxed) state
          • R state has 300x greater affinity for O2
      • exhibits positive cooperativity
        • binding of 1 O2 molecule to 1 subunit of deoxyhemoglobin increases affinity for O2 in adjacent subunits
        • sigmoidal shape of oxygen-hemoglobin dissociation curve is characteristic of positive cooperativity
  • Hemoglobin Variants
    • Hemoglobin F
      • fetal hemoglobin
      • 2 α subunits and 2 γ subunits (α2γ2)
        • ↑ affinity for O2, ↓ affinity for 2,3-BPG
          • facilitates O2 delivery from mother to fetus
    • Hemoglobin S
      • an abnormal variant of hemoglobin that causes sickle cell disease
        • α subunits are normal, β subunits are abnormal
        • forms sickle-shaped robs in red blood cells in deoxygenated form
          • distorts shape of red blood cells
            • can result in occlusion of small blood vessels
      • ↓ affinity for O2
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