Choose the WRONG statement describing the coordination of the iron ion in hemoglobin. The Fe2+ ion is coordinated to the four nitrogen atoms in the center of the protoporphyrin of the heme. The fifth coordination site is occupied by the "proximal histidine" of the globin chain. The oxygen is bound to the sixth coordination site of the iron. Histidine that occupies the fifth coordination site is capable of inhibiting oxidation of the iron to the ferric state.
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The iron ion is coordinated to the four nitrogen atoms in the center of the protoporphyrin of the heme. This statement is correct. Show more…
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Select all statements that correctly describe hemoglobin and myoglobin structure. The heme prosthetic group is entirely buried within myoglobin. Each hemoglobin molecule can bind four oxygen molecules; each myoglobin can bind one oxygen molecule. Both hemoglobin and myoglobin contain a prosthetic group called heme, which contains a central iron (Fe) atom. By itself, heme is not a good oxygen carrier. It must be part of a larger protein to prevent oxidation of the iron. Hemoglobin and myoglobin are heterotetramers. Each iron atom can form six coordination bonds. Two of these bonds are formed between iron and oxygen. Molecular oxygen binds reversibly to the Fe(II) atom in heme.
Sri K.
Which five statements about hemoglobin and myoglobin structure are true? Each hemoglobin molecule can bind four oxygen molecules, and each myoglobin can bind only one oxygen molecule. Molecular oxygen binds irreversibly to Fe2+ in heme. By itself, heme is not a good oxygen carrier. It must be part of a larger protein to prevent a change in the oxidation state of the iron ion. Both hemoglobin and myoglobin contain a prosthetic group called heme, which contains a central iron ion. Heme is composed of an organic protoporphyrin component and a metal ion. Each iron ion can form six coordination bonds: One of these bonds is formed between iron and oxygen. Hemoglobin and myoglobin are heterotetramers.
Adi S.
Both hemoglobin and myoglobin contain a prosthetic group called heme, which contains a central iron (Fe) atom. By itself, heme is not a good oxygen carrier: it must be part of a larger protein to prevent oxidation of the iron. The heme prosthetic group is entirely buried within myoglobin. Each iron atom can form six coordination bonds. Two of these bonds are formed between iron and oxygen. Each hemoglobin or myoglobin molecule can bind four oxygen molecules. Hemoglobin is a heterotetramer, whereas myoglobin is a monomer. Molecular oxygen binds reversibly to the Fe(II) atom in heme.
Prabha S.
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