Physiology · Blood

Hemoglobin: structure, synthesis and functions

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Definition

  • Hemoglobin (Hb) is a conjugated protein pigment in red cells, made of heme (iron-tetrapyrrole) and globin (two pairs of polypeptide chains); comprises more than 90% of red cell dry weight.
  • Normal Hb: adult males 14 to 18 (16 ± 2) g/dL, adult females 12 to 16 (14 ± 2) g/dL.

Structure of Hemoglobin

  • Heme is a tetrapyrrole ring system terminating in protoporphyrin, with a central iron atom; each globin polypeptide chain is bound to one heme moiety to complete the Hb molecule.

Synthesis of Hemoglobin

  • Heme forms in mitochondria, globin in ribosomes; iron and protein deficiency causes Hb deficiency, since both are raw materials.
  • Step 1 Succinyl-CoA (TCA cycle) + glycine → α-amino-β-ketoadipic acid (pyridoxal phosphate) → ALA, via ALA synthase.
  • Step 2 ALA → porphobilinogen → protoporphyrin-IX.
  • Step 3 Protoporphyrin-IX + ferrous iron → heme, via heme synthase.
  • Step 4 Heme + globin → hemoglobin.