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Lecture

BIOCH 200 (February 26, 2014) - Protein Structure and Function & Enzymes

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Department
Biochemistry
Course
BIOCH200
Professor
Walter Dixon
Semester
Winter

Description
BIOCH 200: Protein Structure and Function (con’t) | Enzymes (February 26, 2014) • Allosteric Effectors of Hemoglobin o O 2  Homoallosteric activator o BPG  Heteroallosteric inhibitor for oxygen o H+  Heteroallosteric inhibitor for oxygen • T-State vs. R-State o *T (Tense) State  Has a larger central cavity  Low affinity for oxygen o *R (Relaxed) State  Has a smaller central cavity  Higher affinity for oxygen • BPG (2,3-Biphosphoglycerate) o *Essential for T-state formation and stability o Is a small and highly negative molecule o *Binds to deoxyhemoglobin’s central cavity (lodged between the 4 subunits) o Too big to fit in the central cavity of R-state hemoglobin • H+ ions o Produced from metabolism  *Hydrolysis of ATP and the conversion of carbon dioxide to bicarbonate o 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. Since active skeletal muscles create an environment of a higher pH and myoglobin doesn’t contain a central pocket (and therefore doesn’t undergo a state change), it now has a higher affinity for oxygen than hemoglobin. • The T-state enhances BPG binding and decreases oxygen binding. o Ne
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