- Haemoglobin is a protein in red blood cells that carries oxygen. - The core of each haemoglobin molecule contains four heme groups, each with an iron ion at its center. - In deoxyhaemoglobin (haemoglobin without bound oxygen), the iron ion is in the ferrous state, Fe(II), which is Fe2+. - When oxygen binds to haemoglobin, the iron remains primarily in the Fe(II) state, although the binding process involves some degree of electron redistribution between iron and oxygen. - If the iron is oxidized to the ferric state (Fe3+), the resulting molecule is called methemoglobin, which cannot bind oxygen reversibly and is non-functional for oxygen transport.
In haemoglobin, iron shows which one of the following oxidation states?
Asked in PPSC CS Prelims 2015 · Topic: Food Preservation, Nutrition, Medicine, etc. (Macronutrients: Chemical Structures and Biological Functions (Carbohydrates, Proteins, Lipids))
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