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Structure of Chlorophyll &
      Haemoglobin
Structure of Chlorophyll
• Chlorophyll is a green color pigment
  in green plants and algae.
• It is a magnesium- porphyrin
  complex.
• It is a square planar complex with
  Mg2+ the center .
• The magnesium is at the centre of
  the modified ring septeon (corrin).
• The modified porphyrin acts as the
  ligand.
• It is a naturally occurring chelate
  complex of Mg.
Structure Of
Hemoglobin
• Blood contains red blood corpuscles or
  cells .
• About 95% of the dry weight of the red
  blood cells is composed of hemoglobin ( or
  haemoglobin)
• 100mL of the blood of a normal male
  contains approximately 15g of
  hemoglobin all of which is within the red
  blood cells.
• Haemoglobin contains about 0.35% of iron
  and thus there are 50mg of Fe per 100mL
  blood and 2.5g of iron in the total blood
  volume of 5000ml in an adult man.
• Haemoglobin is a conjugated protein
  having molecular weight of 64,500.
• It is a tetramer in and contains four
  identical units which are arranged
  roughly in a tetrahedron .
• Each unit contains FOUR identical heme
  groups.
• Each hemoglobin molecule has four
  heme groups bound to the globin (a
  protein) on its surface.
• Fe(II) in hemoglobin is in the high spin
  state (Fe2+ = 3d6 =t42g e2g)
• Thus Fe (II) has four unpaired electrons
  in hemeglobin molecule.
• The structure of haemoglobin is an
  octahedral complex of Fe(II).
• The centre of haemoglobin is
  occupied by Fe(II) and the four
  corners of the square base are
  occupied by the four N- atoms of the
  heme group.
• One axial position is occupied by N-
  atom of histidine while the other
  axial positions is occupied by the
  H2O molecule.
Role of hemoglobin in
  biological living
       systems
• Hemoglobin is very sensitive to O2
  and hence readily combines with it
• Thus when we breathe in oxygen,
  hemoglobin (Hb) present in our body
  combines reversibly with the oxygen
  in the lungs to form oxy-hemoglobin
  (HbO2 )
Haemoglobin + O2 ↔ Oxy- hemoglobin
                             + H2 O
(or) Hb + O2 ↔ HbO2 + H2 O
• The formation of HbO2, is called oxy-
  genation of hemoglobin.
• In HbO2, Fe is in +3 oxidation state.
• In the formation of HbO2, H2o molecules
  present at one of the axial positions in
  hemoglobin are reversibly replaced by O2
  molecules.
• As the blood runs through the arteries to
  the tissues, the oxygen pressure decreases
  and oxygen gets bound with the
  hemoglobin is set free.
• This free oxygen diffuses into the body cells
  where it combines with glucose(food) and
  oxidizes it into Carbon di oxide and water.
• Thus oxygen is used in the combustion of
  food.
  C6H12O6 + 6O2 → 6CO2 + 6H20 + 38 ATP

                                      (energy)
• The oxidation of glucose to carbon di oxide is an
  energy releasing process in which energy in the form
  of ATP molecules is produced.
• This energy is utilized by the living organisms to
  perform their various metabolic activities, and for
  maintaining their body temperature.
• Water produced in the above reaction is retained in
  the body while decomposes to give carbon di oxide
  and hemoglobin.
• Carbon di oxide is exhaled out and the haemglobin
  goes to the lungs for reuse.
• The above discussion makes it evident that
  the functions of hemoglobin in our body is to
  supply oxygen to various parts of the body.
• Thus hemoglobin is an oxygen – carrier.
• In the oxygenation of a hemoglobin molecule, a
  proton, (H+ ) is also produced.
• This proton reacts with bicarbonate dissolved in
  the blood to liberate carbon di oxide.

 HCO-3 + H+ ↔ H2 CO3 ↔ H2O + CO2

  CO2 liberated as above is exhausted out.
1. Adva               Refere
         nced In              nces
    Prakas       organic
           h ,G.D.         Chemis
2. Adva           Tuli, S.          try, Vo
        nced In           K.Basu            l II , Sa
                organic          , R.D.M              t ya
                         Chemis           adan.
                                  try, Gu
                                          rudeep
                                                      R aj
Structure of chlorophyll & haemoglobin

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Structure of chlorophyll & haemoglobin

  • 1. Structure of Chlorophyll & Haemoglobin
  • 3. • Chlorophyll is a green color pigment in green plants and algae. • It is a magnesium- porphyrin complex. • It is a square planar complex with Mg2+ the center . • The magnesium is at the centre of the modified ring septeon (corrin). • The modified porphyrin acts as the ligand. • It is a naturally occurring chelate complex of Mg.
  • 4.
  • 6. • Blood contains red blood corpuscles or cells . • About 95% of the dry weight of the red blood cells is composed of hemoglobin ( or haemoglobin) • 100mL of the blood of a normal male contains approximately 15g of hemoglobin all of which is within the red blood cells. • Haemoglobin contains about 0.35% of iron and thus there are 50mg of Fe per 100mL blood and 2.5g of iron in the total blood volume of 5000ml in an adult man.
  • 7. • Haemoglobin is a conjugated protein having molecular weight of 64,500. • It is a tetramer in and contains four identical units which are arranged roughly in a tetrahedron . • Each unit contains FOUR identical heme groups. • Each hemoglobin molecule has four heme groups bound to the globin (a protein) on its surface. • Fe(II) in hemoglobin is in the high spin state (Fe2+ = 3d6 =t42g e2g) • Thus Fe (II) has four unpaired electrons in hemeglobin molecule.
  • 8.
  • 9. • The structure of haemoglobin is an octahedral complex of Fe(II). • The centre of haemoglobin is occupied by Fe(II) and the four corners of the square base are occupied by the four N- atoms of the heme group. • One axial position is occupied by N- atom of histidine while the other axial positions is occupied by the H2O molecule.
  • 10. Role of hemoglobin in biological living systems
  • 11. • Hemoglobin is very sensitive to O2 and hence readily combines with it • Thus when we breathe in oxygen, hemoglobin (Hb) present in our body combines reversibly with the oxygen in the lungs to form oxy-hemoglobin (HbO2 ) Haemoglobin + O2 ↔ Oxy- hemoglobin + H2 O (or) Hb + O2 ↔ HbO2 + H2 O
  • 12. • The formation of HbO2, is called oxy- genation of hemoglobin. • In HbO2, Fe is in +3 oxidation state. • In the formation of HbO2, H2o molecules present at one of the axial positions in hemoglobin are reversibly replaced by O2 molecules. • As the blood runs through the arteries to the tissues, the oxygen pressure decreases and oxygen gets bound with the hemoglobin is set free.
  • 13. • This free oxygen diffuses into the body cells where it combines with glucose(food) and oxidizes it into Carbon di oxide and water. • Thus oxygen is used in the combustion of food. C6H12O6 + 6O2 → 6CO2 + 6H20 + 38 ATP (energy)
  • 14. • The oxidation of glucose to carbon di oxide is an energy releasing process in which energy in the form of ATP molecules is produced. • This energy is utilized by the living organisms to perform their various metabolic activities, and for maintaining their body temperature. • Water produced in the above reaction is retained in the body while decomposes to give carbon di oxide and hemoglobin. • Carbon di oxide is exhaled out and the haemglobin goes to the lungs for reuse.
  • 15. • The above discussion makes it evident that the functions of hemoglobin in our body is to supply oxygen to various parts of the body. • Thus hemoglobin is an oxygen – carrier.
  • 16. • In the oxygenation of a hemoglobin molecule, a proton, (H+ ) is also produced. • This proton reacts with bicarbonate dissolved in the blood to liberate carbon di oxide. HCO-3 + H+ ↔ H2 CO3 ↔ H2O + CO2 CO2 liberated as above is exhausted out.
  • 17.
  • 18.
  • 19. 1. Adva Refere nced In nces Prakas organic h ,G.D. Chemis 2. Adva Tuli, S. try, Vo nced In K.Basu l II , Sa organic , R.D.M t ya Chemis adan. try, Gu rudeep R aj