BIOCHEM 523 Lecture Notes - Lecture 8: Protoporphyrin Ix, Myoglobin, Porphyrin
31 Oct 2017
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Biochem423/523 - lecture 8 - protein function and evolution. Two proteins, myoglobin (mb) and hemoglobin (hb), are members of the globin protein family and involve the acquisition and utilization of oxygen. Myoglobin is primarily found in muscle tissue. Hemoglobin is found circulating in the blood. Hemoglobin also plays a role in removing co2 from tissues. Deep sea creatures have a higher myoglobin concentration to store oxygen. Allosteric effect: a ligand binding at an allosteric site results in structural change in the specialized cells, like human erythrocytes protein, and thereby alters its functional properties. An example of this is the binding of small molecules to hemoglobin. In myoglobin, a single polypeptide chain is folded about a prosthetic group, the heme, Remember that a protein without its prosthetic group bound is said to be a apoprotein. Transition metals help with the binding of o2. An fe chelated to a tetrapyrrole ring system is called a proto-porphyrin ix, a porphyrin.
