oxygen binds irreversibly to this molecule - answer-neither myoglobin or hemoglobin binding pattern for this molecule is considered cooperative - answer-hemoglobin oxygen dissociation curve is hyperbolic in shape - answer-myoglobin oxygen dissociation

oxygen binds irreversibly to this molecule - answer-neither myoglobin or hemoglobin binding pattern for this molecule is considered cooperative - answer-hemoglobin oxygen dissociation curve is hyperbolic in shape - answer-myoglobin oxygen dissociation curve is sigmoidal in shape - answer-hemoglobin this molecule has a greater affinity for oxygen - answer-myoglobin As oxygen binds to this molecule the shape of the molecule changes, enhancing further oxygen binding - answer-hemoglobin carbon monoxide binds at an allosteric site, lowering oxygen binding affinity - answer-neither hemoglobin or myoglobin Select all statements that correctly describe hemoglobin and myoglobin structure. Molecular oxygen binds irreversibly to the Fe(II) atom in heme. Both hemoglobin and myoglobin contain a prosthetic group called heme, which contains a central iron (Fe) atom. The heme prosthetic group is entirely buried within myoglobin. By itself, heme is not a good oxygen carrier. It must be part of a larger protein to prevent oxidation of the iron. Each hemoglobin or myoglobin molecule can bind four oxygen molecules. Hemoglobin is a heterotetramer, whereas myoglobin is a monomer. Each iron atom can form six coordination bonds. One of these bonds is formed between iron and oxygen. - answer-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