The cooperative binding behavior of hemoglobin for oxygen is best explained by...
The cooperative binding behavior of hemoglobin for oxygen is best explained by...
Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
Section: Chapter Questions
Problem 1P
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Question
30.
The cooperative binding behavior of hemoglobin for oxygen is best explained by...
Group of answer choices
The movement of the proximal histidine upon O2 binding causes a structural change at the binding interface between subunits
The oxidation of Fe2+ to Fe3+ and formation of the superoxide ion causes distortion of the protoporphyrin ring, altering binding interface between subunits
The tetrameric nature of hemoglobin's quaternary structure directly confers cooperative binding activity
The movement of the distal histidine upon O2 binding causes a structural change at the binding interface between subunits
The binding of O2 causes a pH shift that changes the protonation state of amino acids located at the interface between subunits
The solubility of hemoglobin in aqueous solution and its insolubility in nonpolar environments
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