Explain the cooperative process of binding of oxygen with haemoglobin.

Short Answer

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The process of oxygen binding to hemoglobin is cooperative, meaning the binding of one oxygen molecule enhances the binding of others. This is due to changes in the conformation of the hemoglobin molecule upon binding of the first oxygen, which facilitates subsequent bindings. The process is visualized as a sigmoidal curve and involves the transition of hemoglobin from the T state (low oxygen affinity) to the R state (high oxygen affinity).

Step by step solution

01

Understanding Haemoglobin and Oxygen

Haemoglobin is a protein in red blood cells that transports oxygen from the lungs to the body's tissues. Each haemoglobin molecule can bind up to four oxygen molecules.
02

Explaining the Cooperativity of Binding

The binding of oxygen to haemoglobin is cooperative, which means that the binding of one oxygen molecule makes it easier for subsequent oxygen molecules to bind. This process is facilitated due to the conformational changes in the protein. When one oxygen molecule attaches to the iron ion in the haemoglobin molecule, it triggers a shape change, called a conformational change, which makes it easier for other oxygen molecules to attach as well.
03

Sigmoidal Binding Curve

The cooperativity of oxygen binding to haemoglobin results in a sigmoidal binding curve. This curve visualizes the saturation of hemoglobin with oxygen as the oxygen concentration increases. Flexibility in binding makes hemoglobin more efficient at capturing oxygen in the lungs and releasing it in oxygen-poor tissues.
04

T State and R State of Haemoglobin

The haemoglobin molecule can exist in two states: T (Tense) state and R (Relaxed) state. In the low oxygen concentration (like in tissues), haemoglobin remains in the T state. When the first oxygen molecule binds, it switches to the R state, which has a higher oxygen affinity. This allows for rapid and efficient loading and unloading of oxygen, thereby maximizing the oxygen supply to tissues.

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