The correct option is D Hb release O2 more readily
The structure of hemoglobin is sensitive to partial pressure of carbon dioxide in addition to partial pressure of oxygen. When circulating hemoglobin encounters an environment where the carbon dioxide levels are elevated, the carbon dioxide decreases hemoglobins affinity for oxygen and oxygen is released to the tissue. Carbon dioxide reduces hemoglobins ability to bind oxygen in two different ways, directly and indirectly. CO2 can bind directly to the amino-terminal ends of the alpha and beta chains that make up the globin. The binding of CO2 to hemoglobin causes a conformational change, reducing hemoglobins hold on oxygen and, as a consequence, oxygen is released. The sensitivity of hemoglobin to carbon dioxide levels can be illustrated on a saturation curve. The saturation curve for hemoglobin shifts to the right as higher carbon dioxide levels are encountered, a phenomenon called the Bohr effect. A shift to the right of the oxygen saturation curve represents a decrease in the affinity of hemoglobin for oxygen.