TRANSPORT OF O2 AND CO2

RONDANG SOEGIANTO

2017

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• External respiration:
Transport of O2 and CO2

• Internal respiration:
Metabolic process within cell
involving utilization of O2 and
release of CO2

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Oxygen delivered from lungs to tissues

Roles:
- ATP biosynthesis
via Respiratory Chain

- Metabolic processes
Hydroxylation by oxygenase

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Generation of CO2 by decarboxylation
Ex: Pyruvate  Acetyl-CoA + CO2
Utilization of CO2:
1. Carboxylation process
- Pyruvate  Oxaloacetate
- Purine biosynthesis
Enzyme: Carboxylase
Coenzyme: Biotin
2. CO2 diffuses to enter blood circulation
Will be exhaled
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Involved with gas transport system:

- Erythrocytes
- Hemoglobin synthesis
- Iron biochemistry
- Formation of Hb

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ERYTHROCYTES

- Body produces ~160 million/min

- Lifespan ~ 110 days
- Biconcave (larger surface than
spherical shape)
- No nucleus
- Produced in bone marrow of flat bones

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Erythropoietin
- Produced by kidney medulla
- Stimulates erythrocyte production
- When O2 is low  hormone >> 
More erythrocytes produced

No mitochondria in RBC
Energy produced via glycolysis  lactate

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HEME SYNTHESIS

Precursors: - Glycine
- Succinyl-CoA

Enzyme: Aminolevulinic acid

synthase (ALA synthase)
Coenzyme: Pyridoxal phosphate
Product: Porphyrin

HEME = Fe-porphyrin
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IRON BIOCHEMISTRY

Fe is transported in blood as protein

complex = TRANSFERRIN

Transferrin produced in liver

Taken up by receptor-mediated endocytosis
Transferrin receptors in RBC >> as the
cell develops

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Iron is stored in RBC as FERRITIN =
Apoferritin (protein) + Fe (inorganic)

RBC destroyed mainly by RETICULO-

ENDOTHELIAL CELLS (REC):
spleen, lymph nodes, bone marrow, liver

Fe reused  biliverdin  bilirubin

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TRANSPORT OF GASES IN BLOOD

Very low solubility of O2 and CO2 

hence carrier is needed

Oxygen carrier: Heme-Protein complex

= Hemoglobin

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Fe2+ but not Fe3+ can bind to oxygen.

Inorganic Fe2+ rapidly oxidized to Fe3+

Not good for oxygen transport

Fe2+ in heme also rapidly oxidized by

oxygen to Fe3+  Hematin
Oxidation also possible by chemicals
Formation of methemoglobin with low
affinity for oxygen.

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Free heme cannot function as O2 carrier
Heme has to bind with protein = Globin

Fe in the heme of hemoglobin is more

resistant to oxidation

Hemoglobin is a tetramer:
4 protein subunits with heme attached
A molecule of Hb binds 4 molecules O2

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Saturation curve of Hb is sigmoid

Saturation curve of myoglobin is

hyperbolic

Myoglobin is not suitable for O2

transport, suitable for O2 storage
Only small release of O2 at PO2
above 20 mm Hg.
With strenuous exercise, drop of PO2
to 5 mg Hg causes release of O2 for
ATP production in mitochondria
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Role of 2,3-Bisphosphoglycerate (2,3-BPG)

1,3 BPG produced in glycolytic pathway

is converted to 2,3 BPG by bisphospho-
glyceromutase

2,3 BPG lowers affinity of Hb for O2

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Bohr Effect

Deoxygenated Hb (reduced Hb) has

higher affinity for oxygen than oxyHb

Proton dissociates from oxygenated Hb

Binding of oxygen releases proton

Binding of proton releases oxygen

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CO2 TRANSPORT

CO2 produced in tissues must be

transported to the lungs

CO2 enters RBC  H2CO3 by enzyme:

carbonic anhydrase

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H2CO3  H+ + HCO3-

Bicarbonate ion moves out of RBC via

ion channel (Band 3) in exchange for Cl-
(anion channel)

The soluble bicarbonate is transported by

serum of venous blood to the lungs.

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Process in lungs to expel CO2 is the reverse
from uptake of CO2 in tissue cells.

Bicarbonate enters alveoli  H2CO3 

H2O + CO2 by carbonic anhydrase

CO2 diffuses out of cell.

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Buffering action

Acid is produced in tissues but pH

of red blood cells must be maintained

Physiological pH is maintained by
buffering power of bicarbonate,
phosphates and hemoglobin.
Bohr effect also buffers.

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Bicarbonate buffer:

Metabolic CO2 reacts reversibly with H2O 

weak acid ( H2CO3). E=carbonic anhydrase

H2CO3  HCO3- (conjugate base)

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Hb acts as buffer thru basic amino acid histidine

Histidine can combine reversibly with H+ 

protonated and unprotonated Hb are formed

this way

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References:

1. MARKS’
Basic Medical Biochemistry. A Clinical
Approach. M. Lieberman, A.D. Marks.
Third ed., 2009
2. Medical Biochemistry. Master Medicine.
A.C. Brownie, J.C. Kernohan 2005.
3. HARPER’S
Illustrated Biochemistry
30th Edition, 2015.

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