Use the information gathered in the Oxygen Binding Proteins Molecular Structure Tutorial to answer the question. Which f
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Use the information gathered in the Oxygen Binding Proteins Molecular Structure Tutorial to answer the question. Which f
question. Which five statements about hemoglobin and myoglobin structure are true? 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. Hemoglobin is a heterotetramer, whereas myoglobin is a monomer. Molecular oxygen binds reversibly to Fe2+ in heme. Each iron ion can form six coordination bonds. Two of these bonds are formed between iron and oxygen. 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 hemoglobin or myoglobin molecule can bind four oxygen molecules.
Use the information gathered in the Oxygen Binding Proteins Molecular Structure Tutorial to answer the