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Hb vs. Mb
Hb vs. Mb: O2 binding
• P50 value: The pO2 at which % saturation = 50% Mb: P50 = 1 Torr
Allosteric Regulation
Mechanism of Cooperativity
Co-operativity:
• Binding of O2 to one haem group affinity of remaining haem groups.
• Allows Hb to deliver 1.83x more O2 than if four sites were independent.
• Increase in affinity is due to Haem interactions
• Affinity of 4th O2 bound = 300x greater than 1st O2 bound.
Oxygenation:
• In deoxy-Hb (tense T-form) the subunits are constrained by eight salt-bridges (non-covalent
electrostatic interactions) – broken on oxygenation.
• the contact region is connected to the haem groups.
• movement at the haem group causes movement at the interface.
• The haem Fe moves further into plane
• The Fe pulls His-F8 towards the haem group
• Movement in the F helix, EF & FG corners
• Rupture of some salt bridges at the interface
• Hb becomes less constrained
Explain the effects of 2,3 BPG and the Bohr effect on Oxygen dissociation.