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Use the information gathered in the Oxygen Binding Proteins Molecular Structure Tutorial to answer the 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.