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Respiratory Physiology, Myoglobin and Hemoglobin Structure and Function

Hemoglobin & Transport of O2 & CO2

Include drawings, equations, graphs, etc. where appropriate.

1. Define the following: prosthetic group, fractional saturation, allosterism, cooperativity, Bohr effect, isohydric carriage, respiratory acidosis & alkalosis, metabolic acidosis & alkalosis. Please provide examples.

2. Describe the interactions (e.g., H-bonding) that are involved in the tight binding of heme to apomyoglobin?

3. Describe Myoglobin's structure (include comments on its primary, secondary, tertiary and quaternary structure).

4. What are the major similarities and differences in structure and properties between myoglobin and hemoglobin? Provide descriptions.

5. What are the structural & functional aspects of the effect of H+ on the O2 binding of hemoglobin? Include any pKa differences, at least one example of a specific functional group involved, etc. What are the consequences of this binding? How does it effect the body in the lungs and in the periphery?

Solution Preview

Hello, here are the responses to your assignment. I don't have access to your exact text book, but you might want to throw some references in there that site your text book.

1. Prosthetic group: these are tightly bound molecules that attach themselves to proteins that are required for some proteins to 'work' within the body. For example, vitamins are prosthetic groups that attach themselves through covalent bonds to some enzymes at the active sites to promote function of the enzyme. Fractional saturation: the amount of available sites on a protein molecule that are actually saturated with a ligand. For example, if a protein has X for the total potential ligand bonds, and Y for the actual sites that are bonded, y/x= the fractional saturation of the protein. Allosterism is when a molecule binds to a site on an enzyme other than the active site, thus changing the shape of the enzyme and disallowing it to bind to its ligand, potentially altering the function of this enzyme. Cooperativity is when an enzyme with multiple ligand binding sites has one ligand bind to it, and then increases or decreases the enzymes affinity for other ligand bonding. The Bohr effect can be defined as the relationship of acidity and concentration of carbon dioxide to hemoglobin's affinity to oxygen. Increasing the bloods concentration with carbon dioxide (lowering the pH and thus increasing acidity) will result in the loss of oxygen from the hemoglobin molecule. The inverse is also true. Isohydric ...

Solution Summary

This is a summary of hemoglobin and myoglobin's structure and function, an explanation of alkalosis and acidosis, prosthetic group, fractional saturation, allosterism, cooperativity, Bohr effect, and isohydric carriage.