As shown in the graph, hemoglobin exchanges oxygen and protons due to an inverse relationship between oxygen binding and proton binding known as the Bohr effect. The binding of oxygen to hemoglobin causes a conformational change that disrupts salt bridges, making oxyhemoglobin more acidic than deoxyhemoglobin. For purposes of calculation, hemoglobin can be modeled as a simple monoprotic buffer, dissociating one proton per subunit as illustrated in the graph and equilibrium equations. pK₂=7.8 HHb — H+ + Hb pK₂=6.7 HHbO₂ H+ + HbO₂ You will now calculate the quantity (in millimoles) of protons that will be released when 1.55 mmol of oxygen binds to deoxyhemoglobin at pH 7.4 and the pH then returns to 7.4 (i.e., going from point A to point B on the curve).
As shown in the graph, hemoglobin exchanges oxygen and protons due to an inverse relationship between oxygen binding and proton binding known as the Bohr effect. The binding of oxygen to hemoglobin causes a conformational change that disrupts salt bridges, making oxyhemoglobin more acidic than deoxyhemoglobin. For purposes of calculation, hemoglobin can be modeled as a simple monoprotic buffer, dissociating one proton per subunit as illustrated in the graph and equilibrium equations. pK₂=7.8 HHb — H+ + Hb pK₂=6.7 HHbO₂ H+ + HbO₂ You will now calculate the quantity (in millimoles) of protons that will be released when 1.55 mmol of oxygen binds to deoxyhemoglobin at pH 7.4 and the pH then returns to 7.4 (i.e., going from point A to point B on the curve).
Chemistry
10th Edition
ISBN:9781305957404
Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
Chapter1: Chemical Foundations
Section: Chapter Questions
Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...
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