BioChemistry > STUDY GUIDE > BioChem C785 - WGU - Module 3 - all questions Answered (All)

BioChem C785 - WGU - Module 3 - all questions Answered

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Hb (hemoglobin) binds to CO (carbon monoxide) with a higher affinity than oxygen and stabilizes the R (relaxed) state - True When hemoglobin changes from the T to the R, it has a high affinity for ... oxygen - True When hemoglobin changes from the R to T, it has a low affinity for oxygen - True Cooperatively refers to - structural changes that increases the affinity for oxygen in hemoglobin When the oxygen concentration is high, the heme shape is planar. When the oxygen concentration is low, the heme shape is bent shape. - True The Bohr effect is a relationship between hemoglobin's oxygen binding behavior in conjunction with the pH of the surroundings. When the pH is low, hemoglobin has low affinity for oxygen and releases oxygen - True Bohr effect is a relationship between hemoglobin's oxygen binding behavior in conjunction with the pH of the surroundings. When the pH is high, hemoglobin has high affinity for oxygen and binds oxygen. - True Relative to the lungs, the pH in the peripheral tissues is lower, because the CO2 generated by metabolism is converted to bicarbonate, which releases proton (H+) - True The Bohr effect is a relationship between hemoglobin's oxygen binding behavior in conjunction with the pH of the surroundings. When the H+ ion concentration increases, the pH of the solution decreases. - True Myoglobin stores oxygen, whereas hemoglobin transports oxygen. Myoglobin has a higher affinity for oxygen compared t [Show More]

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