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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Mitochondrial Mutations

A mitochondrion is a cellular organelle that serves as the site for cellular respiration and energy production (ATP or Adenosine Triphosphate). It is a double-membrane-bound organelle and is only present in eukaryotic cells.