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In: Biology

**Biochemistry** Clearly explain how the structure of hemoglobin is intricately connected to its function, using the...

**Biochemistry**

Clearly explain how the structure of hemoglobin is intricately connected to its function, using the principle listed below as the outline.

  • Small changes in the conformation of a biomolecule can create significant effects within a cell. (consider regulation through allosteric activators or inhibitors, reversible enzyme regulation, substrate/ligand binding, coenzyme or cofactor binding and enzyme mechanisms)

Solutions

Expert Solution

Hemoglobin is a carrier, transporting oxygen from the lungs to the tissues and the return transport of carbon dioxide.

Each hemoglobin molecule is made up of four heme groups surrounding a globin group, forming a tetrahedral structure. Heme, is composed of porphyrin to which an iron atom is attached.

  • Hemoglobin can bind to oxygen by changing its spatial structure from domed to planar.
  • Allosteric effectors such as inositol hexaphosphate (IHP) bind to deoxy Hb and HbCO(carboxy) at different sites, leading to a lowered oxygen affinity
  • hemoglobin ligands include competitive inhibitors such as carbon monoxide and allosteric ligands such as carbon dioxide and nitric oxide. The carbon dioxide is bound to amino groups of the globin proteins to form carbaminohemoglobin. The nitric oxide transport to peripheral tissues is said to assist oxygen transport in tissues, by releasing vasodilatory nitric oxide to tissues in which oxygen levels are low.
  • Also, the binding of oxygen is affected by molecules such as carbon monoxide. CO competes with oxygen at the heme binding site and Hemoglobin binding affinity for CO is 250 times greater than for oxygen that means small amounts of CO can reduce hemoglobin ability to deliver oxygen to the target tissue.
  • The binding of Oxygen by hemoglobin is regulated by H+, Carbon dioxide and 2,3-bisphosphoglycerate

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