Lec15 - MIDTERM RESULTS Average 267(B Std:72 Median 272...

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MIDTERM RESULTS Average: 267 (B-) Std.:72 Median: 272 Highest:425 Lowest: 60
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Oxygen Binding to Hb Binding is Cooperative
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Quaternary Conformations of O2 Bound and Unbound Hb are Different
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A small change in Fe2+ Coordination geometry
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Mechanism of Oxygen Binding
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Mechanism of Oxygen Binding Oxygen Unbound: (T State) Fe2+ is out of the Heme Plane Oxygen Bound: (R State) Fe2+ is in the Heme Plane Subunit Interfaces Alters
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α 1: β 2 ( α 2: β 1) interface T vs R State
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T State vs R State
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Ionic interaction between N & C Termini
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Decrease in pH reduces the affinity for O 2 Protonation of Hb at low pH N-amino group ( α subunits) C-terminal His ( β subunits) When protonated, these groups are involved in ion-pairs that stabilize the T form (deoxy-Hb) Bohr effect
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Hb releases 0.6 units of proton upon O 2 binding. That is, Hb binds O 2 better at higher pH (low proton) R state is more stable at high pH
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Blood-Lung Oxygen transport Cycle
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Lung High pH • Low pCO 2 • High pO 2 • O 2 binding Tissue Low pH • High pCO 2 • Low pO 2 • O 2 release
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H + production in tissues CO 2 + H 2 O H + + HCO 3 - Lactic acid H + + Lactate -
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O 2 H + CO 2
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This note was uploaded on 10/28/2010 for the course CHEM 114A taught by Professor Viadhiu during the Fall '08 term at UCSD.

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Lec15 - MIDTERM RESULTS Average 267(B Std:72 Median 272...

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