Willmott 8 Myoglobin and Haemoglobin Flashcards
Haemoglobin
function:
size:
form:
- Oxygen-carrying protein in red blood cells (easily acessable)
- Tetramer with polypeptide chains in α2β2 complex:
- α type = 141 amino acids β type = 146 amino acids (all helixes)
- Contains essential prosthetic group (haem - with Fe atom)
Haemoglobin
saturation curve
• SigmoidalO2-bindingcurve (cooperativity)
Hb – pathway of communication
- O2 binds to Fe2+
- Fe2+ moves 0.7 Angstrom into plane of ring
- Pulls Histidine side chain towards ring
- Histidine residue is in F-helix which moves by several
- Breaks interactions (electrostatic) at subunit interface allowing relative rotation of subunits
O2 binding to Hb affected by…
• H+ favours deoxy form (acidic conditions)
• CO2 favours deoxy form
• BPGbinds1pertetramer (biphosphoglycerate)
• stabilises deoxy form
• All these effectors promote O2 release in tissues
Lactate acid effect
= acidic => favour O2 release
Oxygenation of Hb
Moves Fe 2+ into centre of porphyrin ring
BOHR EFFECT
25% drop max binding by pH
Two effects of CO2 on Hb
• Generates H+ (acid) • binds directly to Hb amine groups CO2 + H2O H2CO3 H+ + HCO3- Carbonate ion -NH2 + CO2 -> N COO- H Carbamate ion
bis =
2P bonded separatley to C backbone
BPG effect on Hb
Reduces affinity of Hb for O2
Foetal haemoglobin
subunit strucutre:
function:
amino a difference:
• α2γ2 subunit structure
• Binds BPG less tightly than adult Hb (α2β2 )
• Therefore binds O2 more tightly than adult Hb
• Oxygen can pass from mother’s blood to foetus
gamma chains
Ser 143 NOT His 143 -> not same +/ve charge => favour oxygenated state
Sickle cell anaemia
- Disease caused by defective Hb
- point mutation in β chain (Glu6 to Val) A-> T -/ve -> non-polar => hydrophobic -> hydrophobic
• Leads to loss of solubility and precipitation in red blood cells
Heterozygous individuals have
increased resistance to Malaria
Tripsin =
protease in sequence preference to cut 2D chromatography