Hemoglobin_and_myoglobin_1

Hemoglobin_and_myoglobin_1 - Chemistry 233 Fundamentals of...

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Chemistry 233 Fundamentals of Biochemistry Myoglobin and Hemoglobin 1
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Myoglobin and Hemoglobin What is QUATERNARY STRUCTURE? How does quaternary structure work? How do myoglobin and hemoglobin work? a. on a molecular basis b. on a physiological basis
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Myoglobin (Mb) O 2 carrying protein in the muscle O 2 -binding cofactor: heme protein: globin protein is 80% α -helical helices A Æ H 153 amino acids
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heme cofactor is a porphyrin or tetrapyrrole binds Fe 2+ in the center which is the site of O 2 binding
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Where does the O 2 bind? heme binds to the protein between the E and F helices HisF8 coordinates the Fe 2+ HisE7 does not coordinate Fe 2+ but restricts the size of the O 2 binding site
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Space-fill view of O 2 binding to Myoglobin
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The globin modifies the O 2 binding properties of heme: compare binding of CO to free heme vs binding of O 2 and CO to heme in Mb.
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CO binds at an angle and not as tightly to the Fe 2+ in myoglobin (relative binding = 200 as compared to binding to free heme) O 2 binds at an angle and even less tightly to in myoglobin (relative binding = 1) **hindered binding of O 2 to hemein myoglobin prevents oxidation of the Fe (important!) ** CO binds perpendicular to Fe and very tightly to free heme (relative binding = 20,000) reversible O binding
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This note was uploaded on 03/12/2009 for the course CHEM 233 taught by Professor Daub during the Winter '09 term at Waterloo.

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Hemoglobin_and_myoglobin_1 - Chemistry 233 Fundamentals of...

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