In the lungs, the highly saturated oxygen environment can overcome the lower affinity T-form of hemoglobin, effectively binding despite disadvantageous binding capacity. This structural change to the taut form leads to low-affinity hemoglobin, whereas the relaxed form leads to a high-affinity form of hemoglobin with respect to oxygen binding. Hemoglobin exists in 2 forms, the taut form (T) and the relaxed form (R). This configuration shift of hemoglobin under the influence of protons is classified as the taut (T) form. Specifically, it is the association of protons (H+ ions) with the amino acids in hemoglobin that cause a conformational change in protein folding, ultimately reducing the affinity of the binding sites for oxygen molecules. These effects decrease hemoglobin’s affinity for oxygen, weakening its binding capacity and increasing the likelihood of dissociation this is represented as a rightward shift of the hemoglobin dissociation curve, as hemoglobin unloads oxygen from its binding sites at higher partial pressures of oxygen. This increase in tissue PCO2 leads to an increase in hydrogen ion (H+) concentration, represented as a decrease in pH as the environment undergoes the process of acidosis. Through the biochemical reactions necessary for cellular respiration, increases in metabolic activity within tissues result in the production of carbon dioxide (CO2) as a metabolic waste product.
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