Chapter7 - Chapter 7 Hemoglobin Lecture overview 1 2 3 4 Mb...

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Chapter 7: Hemoglobin 1. Mb and Hb bind oxygen using heme 2. Hb is cooperative in its binding 3. The Bohr effect 4. Mutations of Hb subunits can cause disease Lecture overview
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-A single species, in its effort to utilize energy, pollutes the earth by producing a small gaseous molecule that is toxic to most other living organisms, causing a massive extinction of species and a biological catastrophe .....
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The History of Oxygen Transport Oxygen Transporters Photosynthesis = O 2 Fe 2+ to Fe 3+ cytochrome oxidase
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What kinds of proteins have evolved to transport oxygen? Arthropods, mollusks Hemocyanins Some marine worms and bivalves Animals, plants, and some bacteria Hemoglobins Hemerythrins
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Hemoglobin is found in the red blood cells and is the major O 2 carrying molecule of vertebrates. In lungs, hemoglobin binds O 2 . In muscles and other metabolizing tissues, hemoglobin releases O 2 and myoglobin binds O 2 . How do these proteins bind and release O 2 in a controlled reversible manner? Hemoglobin xample of protein structure and function:
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Facilitated Diffusion Kinetics, Affinity, and Transport are Linked Hb+O HbO k k K = k k k > 1 s K : Hb < Mb < Mitochondria [Hm] > 1 mM
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+ = Apo-globin Fe (III) “oxidized” Fe (II) “reduced” O 2 , CO, NO Anions, NO What does the protein and heme parts of hemoglobin do? Holo-globin (Red)
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“Heart of Steel” (2005) sculpture of Hb by Julian Voss Andreae demonstrates the oxidation of hemoglobin in a graphic way. The protein slows the oxidation of the heme iron….
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Originally it was thought that steric hindrance played a role (Perutz was wrong!), but now it is believed that H-bonding with the distal His is the most important factor (this is how it slows oxidation too).
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