What is biological function and metal center of haemoglobin
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Explanation:
The heme group (a component of the hemoglobin protein) is a metal complex, with iron as the central metal atom, that can bind or release molecular oxygen. Both the hemoglobin protein and the heme group undergo conformational changes upon oxygenation and deoxygenation.
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Hemoglobin is made up of two pairs of globin chains and four metalloporphyrins, which contain iron.
What is hemoglobin?
- Red blood cells include the protein hemoglobin, which delivers oxygen to your body's organs and tissues and carbon dioxide from those tissues back to your lungs.
- You have a low red blood cell count if a hemoglobin test finds that your hemoglobin level is lower than normal (anemia).
- Hemoglobin is a two-way respiratory carrier that carries carbon dioxide back to the lungs while also carrying oxygen from the lungs to the tissues.
- Hemoglobin has a high affinity for oxygen in the arterial circulation but a poor affinity for carbon dioxide, organic phosphates, hydrogen, and chloride ions.
Heme group in Hemoglobin:
- A core iron atom complexed with four nitrogen atoms makes up the heme group.
- The process of oxygenation allows oxygen to attach to the heme unit in a way that is reversible.
- Cooperativity describes how a hemoglobin molecule's subunits interact with one another.
- Because there is an iron atom in the heme group, myoglobin and hemoglobin may bind oxygen.
- Additionally, it adds to the red hue of blood and muscles.
- An iron atom can attach to one oxygen (O2) molecule inside each heme group.
- Four oxygen molecules can be bound by each hemoglobin protein.
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