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Describe how cooperativity of oxygen binding in hemoglobin is advantageous for the transport of oxygen from the lungs to the tissues and why myoglobin would not be a good protein to use for the oxygen transport

Respuesta :

The affinity of hemoglobin for oxygen is less than its structural analog myoglobin. However, this does not affect hemoglobin's usefulness for the body; on the contrary, it allows hemoglobin to be a  more efficient carrier than myoglobin. This is because hemoglobin can release oxygen more easily than can myoglobin. It is both important for oxygen to be carried to different areas and also to be released when needed. The higher affinity of a given protein for oxygen, the harder it will be for that protein to release oxygen when needed. Therefore, hemoglobin's lower affinity for oxygen serves it well because it allows hemoglobin to release oxygen more easily in the body. 
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Due to the nature of each protein molecule, the cooperativity of oxygen binding in hemoglobin allows for the greater transport of oxygen from the lungs to the tissues.

Myoglobin binds oxygen too tightly and releases it very slowly, thus, it is not a good protein for oxygen transport.

What are haemoglobin and myoglobin?

Haemoglobin is the oxygen carrying molecule present in red blood cells.

Myoglobin is the oxygen storage molecules present in muscle cells.

Cooperativity of oxygen binding refers to the increase in the ability of haemoglobin to bind oxygen after binding of the first oxygen molecule.

Cooperativity of oxygen binding in hemoglobin allows for the greater transport of oxygen from the lungs to the tissues.

Myoglobin binds oxygen too tightly and releases it very slowly, thus, it is not a good protein for oxygen transport.

Learn more about haemoglobin and myoglobin at: https://brainly.com/question/1596657

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