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2. Hemoglobin releases protons upon oxygen binding. This phenomenon is called the Bohr effect, and an important group that participates is histidine 146 of the B subunit. In deoxyhemoglobin histidine 146 forms a salt bridge with aspartic acid 94. CH 'N. C-O- *HN `CH, The salt bridge is disrupted upon oxygenation: deoxyhemoglobin oxyhemoglobin his146 asp94 asp94 his146 The pKa of the histidine side group in the deoxy form is higher than that in the free amino acid, but changes upon oxygenation of the heme Fe(II) atom. How does the pKạ change (i.e., Bi214 Lab 3 Report 1 does it increase or decrease)? Why does this change occur?

2. Hemoglobin releases protons upon oxygen binding. This phenomenon is called the Bohr effect, and an important group that participates is histidine 146 of the B subunit. In deoxyhemoglobin histidine 146 forms a salt bridge with aspartic acid 94. CH 'N. C-O- *HN `CH, The salt bridge is disrupted upon oxygenation: deoxyhemoglobin oxyhemoglobin his146 asp94 asp94 his146 The pKa of the histidine side group in the deoxy form is higher than that in the free amino acid, but changes upon oxygenation of the heme Fe(II) atom. How does the pKạ change (i.e., Bi214 Lab 3 Report 1 does it increase or decrease)? Why does this change occur?

Human Anatomy & Physiology (11th Edition)
Human Anatomy & Physiology (11th Edition)
11th Edition
ISBN:9780134580999
Author:Elaine N. Marieb, Katja N. Hoehn
Publisher:Elaine N. Marieb, Katja N. Hoehn
Chapter1: The Human Body: An Orientation
Section: Chapter Questions
Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...
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2. Hemoglobin releases protons upon oxygen binding. This phenomenon is called the Bohr effect, and an important group that participates is histidine 146 of the B subunit. In deoxyhemoglobin histidine 146 forms a salt bridge with aspartic acid 94. CH 'N. C-O- *HN `CH, The salt bridge is disrupted upon oxygenation: deoxyhemoglobin oxyhemoglobin his146 asp94 asp94 his146 The pKa of the histidine side group in the deoxy form is higher than that in the free amino acid, but changes upon oxygenation of the heme Fe(II) atom. How does the pKạ change (i.e., Bi214 Lab 3 Report 1 does it increase or decrease)? Why does this change occur?
Transcribed Image Text:2. Hemoglobin releases protons upon oxygen binding. This phenomenon is called the Bohr effect, and an important group that participates is histidine 146 of the B subunit. In deoxyhemoglobin histidine 146 forms a salt bridge with aspartic acid 94. CH 'N. C-O- *HN `CH, The salt bridge is disrupted upon oxygenation: deoxyhemoglobin oxyhemoglobin his146 asp94 asp94 his146 The pKa of the histidine side group in the deoxy form is higher than that in the free amino acid, but changes upon oxygenation of the heme Fe(II) atom. How does the pKạ change (i.e., Bi214 Lab 3 Report 1 does it increase or decrease)? Why does this change occur?
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