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?

Name: 2. Hemoglobin releases protons upon oxygen binding. This phenomenon i
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Description: 2. Hemoglobin releases protons upon oxygen binding. This phenomenon is called the Bohreffect, and an important group that participates is histidine 146 of the B subunit. Indeoxyhemoglobin histidine 146 forms a salt bridge with aspartic acid 94.CH'N.

Biology: The Dynamic Science (MindTap Course List)

4th Edition

ISBN:9781305389892

Author:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Publisher:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Chapter7: Cellular Respiration: Harvesting Chemical Energy

Section: Chapter Questions

Problem 7TYK

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