Structure Of Hemoglobin
V.S.RASHMI PRIYEM
ULTRA’S BEST DENTAL
SCIENCE COLLEGE
HEMOGLOBIN
• CONJUGATED PROTEIN
• CONTAINING HEME AND GLOBIN
• TETRAMERIC ALLOSTERIC PROTEIN
HEME
• NON PROTEIN PART
• PROSTHETIC PART
GLOBIN
• APOPROTEIN PART
RBCs
• RED BLOOD PIGMENT IN ERYTHROCYTES
NORMAL CONCENTRATION
• MALES
▫ 14-16 g/dL
• FEMALES
▫ 13-15 g/dL
BIOCHEMICAL FUNCTION
• ASSOCIATED WITH RESPIRATION
• DELIVERY OF O2 FROM LUNG TO TISSUES
• TRANSPORT OF CO2 AND PROTONS FROM
TISSUES AND LUNGS
SHAPE
• HEMOGLOBIN IS GLOBULAR IN SHAPE
HbA
• MADE UP OF
▫ 2 α CHAINS
▫ 2 β CHAINS
• NORMAL BLOOD CONTAINS 97% HbA
HbA2
• MADE UP OF
▫ 2 α CHAINS
▫ 2 δ CHAINS
• NORMAL BLOOD CONTAINS 2% HbA2
HbF
• MADE UP OF
▫ 2 α CHAINS
▫ 2 γ CHAINS
• NORMAL BLOOD CONTAINS 1% HbF
GENES RESPONSIBLE
• ALPHA CHAIN GENE IS PRESENT ON
CHROMOSOME 16
• BETA, GAMMA AND DELTA CHAIN GENES
ARE PRESENT ON CHROMOSOME 11
AMINO ACIDS
• EACH ALPHA CHAIN HAS 141 AMINO ACIDS
• EACH BETA, GAMMA AND DELTA CHAINS
HAVE 146 AMINO ACIDS
• ON A TOTAL HEMOGLOBIN CONTAINS 574
AMINO ACIDS
STRUCTURE OF HEME
• CONTAINS PORPHYRIN RING
• CONSISTS OF 4 PYRROLE RINGS LINKED BY
METHYLENE BRIDGES
• WITH IRON(FERROUS STATE) AT ITS
CENTER
STRUCTURE OF GLOBIN
• CONSISTS OF 4 POLYPEPTIDE CHAINS
• CONTAINS 574 AA RESIDUES
BUFFERING ACTION
• CONTAINS 36 HISTIDINE RESIDUES
• IMP. IN BUFFERING ACTION
DISTAL HISTIDINE
• 58TH AA IS HISTIDINE
• KNOWN AS DISTAL HISTIDINE
• AWAY FROM IRON ATOM
PROXIMAL HISTIDINE
• 87TH AA IS HISTIDINE
• KNOWN AS PROXIMAL HISTIDINE
• NEAR TO IRON ATOM
BONDING
• 4 SUBUNITS HELD TOGETHER BY NON-
COVALENT INTERACTIONS
• HYDROPHOBIC, IONIC AND HYDROGEN
BONDING
HYDROPHOBIC CLEFT
• THERE ARE 4 HEME RESIDUES PER Hb, ONE
FOR EACH SUBUNIT IN Hb
• HEME IS LOCATED IN A HYDROPHOBIC
CLEFT OF GLOBIN CHAIN

Structure of Hemoglobin