Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
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Question
Chapter 7, Problem 11P
Interpretation Introduction
Interpretation:
The usage of the structural change in the oxygen carriers present in arthropods to facilitate cooperative oxygen binding is to be stated.
Concept introduction:
Proteins are the
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A variant of hemoglobin (Boston variant; mutation His E7(58)α → Tyr) promotes methemoglobin formation involving the α (alpha) subunits. What is the maximum value of the Hill constant (n) that you could measure for the Boston variant of hemoglobin?
log (YO2 / 1 - YO2 ) = log pO2 - logP50
Please break down each step of the Hill equation and explain why the result for n is valid from a logical standpoint.
384
Structure and Function of Hemoglobin
Q4.4- In addition to O2, another diatomic molecule that can bind to the iron atom in hemoglobin is CO. Explain in biochemical terms why high levels of CO gas are lethal and cite a specific example of accidental death by CO poisoning (where/when/how).
Recall from your BI110 class that metabolically active tissues produce CO2 as a by-product of cellular respiration. Those metabolically active tissues require the O2 that is brought by hemoglobin for the same process (cellular respiration). Explain why the effect of pH on hemoglobin’s affinity for oxygen is consistent with delivering it to actively metabolizing tissues. (Hint: think about what effect the presence of CO2 has on the tissues…)
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- ROS, not ROUS. What are the reactive oxygen species and why are they especially dangerous to cells?arrow_forward30. 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 environmentsarrow_forward(No more than one page). Explain why quaternary structure is necessary for cooperativity and allosteric regulation. Use hemoglobin as an example. Include the various allosteric effectors that influence oxygen binding.arrow_forward
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