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Description: Describe the structural basis for the cooperative (allosteric) binding of O2 by hemoglobin but not by myoglobin

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Biochemistry

Describe the structural basis for the cooperative (allosteric) binding of O2 by hemoglobin but not by myoglobin

Human Heredity: Principles and Issues (MindTap Course List)

11th Edition

ISBN:9781305251052

Author:Michael Cummings

Publisher:Michael Cummings

Chapter10: From Proteins To Phenotypes

Section: Chapter Questions

Problem 18QP

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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.

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Describe the structural basis for the cooperative (allosteric) binding
of O2 by hemoglobin but not by myoglobin

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Structure of hemoglobin and myoglobin

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Binding of Oxygen to myoglobin and hemoglobin

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Under appropriate conditions, hemoglobin dissociates into its four subunits. The isolated α subunit binds oxygen, but the O2 -saturation curve ishyperbolic rather than sigmoid. In addition, the binding of oxygen to the isolated α subunit is not affected by the presence of H+, CO2 , or BPG. What do these observations indicate about the source of the cooperativity in hemoglobin?
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