ch05.2 - The Bohr effect, the effect of pH and CO 2...

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Unformatted text preview: The Bohr effect, the effect of pH and CO 2 concentration on the binding and release of oxygen by hemoglobin, dictates that A. oxygen binds hemoglobin better at low pH. B. oxygen and H + are bound at the same sites in hemoglobin. C. the binding of CO 2 is inversely related to the binding of oxygen. D. the binding of CO 2 is inversely related to the binding of H + . 5-3, 2 His-93 (F8) His-64 (E7) His-93 (F8) Structural properties of heme binding in Mb " = pO 2 P 50 + pO 2 = 0.26 kPa for Mb 5-4b MbO 2 Mb + O 2 Saturation curve for Mb-oxygen binding 5-10 Structure of Hb, an oligomeric protein (has 4 oxygen binding sites) 5-6 Mb and Hb subunits have similar backbone structures Compare oxygen binding characteristics of Mb and Hb: cooperativity sigmoidal What is the shape of the Mb curve? hyperbolic What is the shape of the Hb curve? V&V10-3 ( ) = Hill plot slope, n = degree of interaction between sites Plot log( " 1 #" ) vs. log [L] 5-14 Advantages of Bohr effect: O 2 Hb + H + + CO 2 + O 2 Hb H + CO 2 lungs ( pH, CO 2 ) tissues ( pH, CO 2 ) Note: Mb does not show any Bohr effect. Protein Function Myoglobin and Hemoglobin Chapter 5 Which of the following is true about the T (tense) R (relaxed) transition of hemoglobin? A. The T state of hemoglobin binds oxygen with a higher affinity than the R state. B. The binding of O 2 to a subunit in the T state can cause the transition of other subunits to the R state. C. The T state has a narrower pocket between the subunits than does the R state....
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This note was uploaded on 11/02/2009 for the course CH 302 taught by Professor Holcombe during the Spring '07 term at University of Texas at Austin.

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ch05.2 - The Bohr effect, the effect of pH and CO 2...

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