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Hemoglobin-Structure & Function (2)

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8 views41 pages

Hemoglobin-Structure & Function (2)

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suriyashankaran042007
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© © All Rights Reserved
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Hemoglobin

Structure & Function

Dr.Pavithra M.B.B.S., M.D


Assistant Professor
HEMOGLOBIN
• Protein – made up of heme (prosthetic group) & globin chain
(polypeptide)

• Quaternary structure

• Transport of oxygen
Component of Hemoglobin
• 4 Heme
– 4 Porpyrole ring
– 4 Iron
• Reduced state = Ferrous(Fe++)
• One Fe+2 in middle of each Porphyrin ring

• 4 Globin Chain
Structure of Heme
Structure of Globin

• Protective hydrophobic pocket for binding of heme that protects the

reduced form (Fe2+ ) of iron from oxidizing to ferric form (Fe 3+ )

• 2 alpha(α), 2 beta(β) / 2 gamma(γ) / 2 delta(δ) / 2 epsilon(ε)

• Alpha chains – 141 amino acids and Beta – 146 amino acids

• 36 Histidine residues – responsible for buffering action


Hemoglobin
Structure
Linkage of heme with globin
Structure
• Adult Hb (HbA) = 2α + 2β chains.
• Fetal Hb (HbF ) = 2α + 2γ chains.
• HbA2 = 2α + 2δ chains.
• Normal adult blood
– 97% HbA
– 2% HbA2
– 1% HbF.
• Normal level of hemoglobin (Hb) in blood :
In males : 14-16 g/dl
In females : 13-15g/dl
Functions of Hemoglobin

• Imparts red colour to the blood

• Oxygen transport from lungs to the tissues

• Transport CO2 from the tissues to the lungs

• Buffers the blood pH by acid base regulation


1.Oxygen transport
• 4 heme residues – iron in ferrous state

• Each heme combines with one molecule of O2

• Oxygenated Hb - iron is in reduced state, take up oxygen


in lungs and release to the tissues

• Deoxygenated Hb – peripheral tissues oxygen is released


Quaternary structure of Hemoglobin
Oxygen dissociation curve

• The ability to load and unload oxygen at physiological pH is shown by


ODC
Oxygen dissociation curve
• At a pO2 of 100 mmHg, hemoglobin is 100% saturated

• At a pO2 of 40 mmHg, hemoglobin is 75% saturated

• At a pO2 of 25 mmHg, hemoglobin is 50% saturated. The partial pressure


of oxygen at which the hemoglobin is 50% saturated is also known as
P50.
Factors affecting ODC
1. Heme-heme interaction cooperative binding

2. Effect of pH and pCO2

3. Bohr effect

4. Chloride shift

5. Effect of temperature

6. Effect of 2,3 BPG


Cooperative oxygen binding of Hemoglobin

• Binding of first oxygen to heme of hemoglobin enhances the binding


of oxygen to remaining heme of same molecule of hemoglobin

• Homotropic interaction and this enhances enhances oxygen transport


Oxygen dissociation curve – sigmoidal (S) shaped because of cooperative
binding
Effect of pH and pCO2

• Hemoglobin transports significant amount of H + & CO2 from tissues to


the lungs and kidney

• Binding of H+ & CO2 – decreases binding of O2

• At low pH (increased H+ ) & elevated pCO2 in peripheral tissues,

affinity of Hb for O2 is decreased & vice versa

• Effect – Bohr effect


Bohr effect
Chloride shift / Hamburger effect

• In tissues - CO2 enters the venous blood & diffuses into RBCs

• Bicarbonate increases – diffuse out of plasma

• Chloride ions from plasma enters tissues

• In lungs – vice versa


Chloride shift in tissues & in lungs
Effect of temperature

• ODC – shift to left at low temperatures

• Febrile conditions – shift to right at high temperatures


Effect of 2,3 BPG

• Intermediate in glycolytic pathway

• Binds to beta chains of deoxy Hb and stabilizes T form

• During oxygenation – it is released from the Hb


Effect of 2,3 BPG

• Decreases the binding of O2 – unloading of oxygen

• In deprivation conditions – 2,3 BPG increases

• ODC – shift to right

• Fetal hemoglobin has more affinity to oxygen than adult – Why?


Carbon monoxide poisoning

• CO binds tightly to hemoglobin form – carboxyHb

• 220 times greater affinity than oxygen

• CO binds to heme sites – Hb shifts to R form

• ODC – left (Hyperbola shape)


Types of Hemoglobin
Transport of Carbon dioxide
• Dissolved form – 10%

• Isohydric transport – 75%

• Carriage as Carbaminohemoglobin – 15%


Discussion
• Hemoglobin structure

• Functions of Hb

• Cooperative binding

• Bohr effect

• Chloride shift

• 2,3 BPG

• Different types of HB
MCQs
1. How many heme groups are present in a single hemoglobin molecule?

a) 1
b) 2
c) 4
d) 8

c) 4
MCQs
2. Adult hemoglobin (HbA) is a tetrameter consisting of

a) α2β2

b) α2δ2

c) α2γ2

d) β4

a) α2β2
MCQs
3. Which of the following is the oxygen binding site of the hemoglobin?

a) HbA shows hyperbolic oxygen dissociation curve

b) HbA shows a sigmoidal oxygen dissociation curve

c) T-state favors the oxygen binding to hemoglobin

d) R-state favors the oxygen binding to hemoglobin

b) HbA shows a sigmoidal oxygen dissociation curve


d) R-state favors the oxygen binding to hemoglobin
MCQs
4. Identify the correct statements regarding hemoglobin (HbA) from the following
options

a) N-terminal of the beta subunit

b) Carboxyterminal of both alpha and beta subunits

c) Ferric ion (Fe+3) of the heme molecule

d) Ferrous ion (Fe+2) of the heme molecule

d) Ferrous ion (Fe+2) of the heme molecule


MCQs
5. Which of the following allosteric regulators favor the unloading of oxygen in
the peripheral tissues?

a) Low pH

b) Low 2-3 Bisphosphoglycerate

c) Low partial pressure of carbon dioxide

d) All of the above

a) Low pH
Short notes

1. Structure and Functions of Hemogobin


References

1. DM Vasudevan – Textbook of Biochemistry; 10th edition

2. Pankaja Naik – Biochemistry; 6th edition

3. Dinesh Puri – Textbook of Medical Biochemistry; 5 th edition

4. Rafi MD - Textbook of Biochemistry; 3rd edition


THANK YOU

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