BIOCH200 Lecture Notes - Myoglobin, Hemoglobin, Hydrolysis
10 Apr 2014
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Bioch 200: protein structure and function (con"t) | enzymes (february 26, 2014: allosteric effectors of hemoglobin, o2. Heteroallosteric inhibitor for oxygen: t-state vs. r-state, *t (tense) state. Low affinity for oxygen: *r (relaxed) state. *hydrolysis of atp and the conversion of carbon dioxide to bicarbonate: lower ph as a result of increase [h+] causes protonation of the side chains and causes hemoglobin to have a lower affinity for oxygen. *hemoglobin then releases the oxygen molecule and myoglobin picks it up. *carbon dioxide is transferred to the lungs via two routes: conversion to bicarbonate, conversion to carbamate. * -chain glu6 is replaced by val: this is a critical substitution! Because of this mutation, the hydrophobic val protein binds to it and causes hb to aggregate into long fibers: which may also pierce the membrane of rbcs. Hemoglobin is stuck between the t and r states: *ex.
