Vous êtes sur la page 1sur 5

BIOCHEMISTRY OF HEMOGLOBIN OXIDATION-REDUCTION

A. HEMOGLOBIN FORMATION

 Heme : a cyclic tetrapyrrole consisting of
four molecules of pyrrole linked by
methyne bridges  absorb visible light 
colors heme deep red
 Hemoglobin : a tetramer composed of two
different types of subunits

 The tetrameric structure of hemoglobin facilitates saturation with O2 in the lungs and release of
O2 as it travels through capillary beds

B. OXYGEN DISSOCIATION CURVES
 Myoglobin curve : hyperbolic
 Hemoglobin curve : sigmoidal (seperti huruf S)
Interpretation
When Po2 is high (in lungs)  both myoglobin and hemoglobin saturated with O2
When Po2 is low (in oxygen-using tissues)  hemoglobin can’t bind oxygen as well as myoglobin
 myoglobin is a good oxygen-storage, hemoglobin is a good oxygen-vehicle

04 nm beyond it  transmitted to the proximal (F8) histidine  rupture of salt bridges between carboxyl terminal residues  one pair of alpha/beta subunits rotates 15°  The cooperativity in O2 binding in Hb comes from conformational changes in tertiary structure that take place when O2 binds  Conformational changes : changing from a T (tense) state with low affinity for O 2 to an R (relaxed) state with a high affinity for O2 . OXYGENATION-DEOXYGENATION OF HEMOGLOBIN : CONFORMATIONAL CHANGES  The binding of teh first O2 molecule to deoxyHb shifts the heme iron toward the plane of the heme ring from a position about 0.C.

HEMOGLOBIN TRANSPORTS CO2 AND PROTONS TO THE LUNGS  After delivering O2 to the tissue  Hb transport CO2 and protons to the lungs  CO2 carries as carbamates  carbamate changes the charge on amino terminals from positive to negative  favoring salt bridges formation  CO2 in venous blood : 15% as carbamate. AGENTS THAT AFFECT OXYGEN BINDING 1. remain as bicarbonate  The Bohr Effect : “hemoglobin’s oxygen binding affinity is inversely related to both acidity and to the concentration of carbon dioxide”  Protons for the Bohr effect arise from rupture of salt bridge E.3-Bisphosphoglycerate  Formed in red blood cells . 2.D.

3-BPG 2. proses diatas terjadi terbalik. Oxygen berikatan dengan Hb  release protons  combine with bicarbonate to form carbonic acid In tissues : pH of the blood is low because of the CO2 produced by metabolism  O2 released from Hb In lungs : pH of the blood is higher because CO2 is being exhaled  O2 binds to Hb 3. some of it (15%) covalently bound to Hb as carbamate  In the lungs : Po2 is high  oxygen binds to Hb and CO2 released .  Binds to HB in the central cavity formed by the four subunits  increasing the energy required for the conformational changes that facilitate oxygen binding  lowers the affinity of Hb for oxygen  oxygen is readily bound when Hb contains 2. Proton Binding (Bohr Effect)  Binding of protons  lowers its affinity for oxygen  pH of blood decrease as it enters the tissue (because CO2 produced by metabolism converted to carbonic acid)  Dissociation of carbonic acid produce protons  react with several amino acid residues in Hb  conformational changes that promote the release of O2  In the lungs. Carbon Dioxide  Most of CO2 to the lungs as bicarbonate.