The O2-binding curve for Hemoglobin (Hb) is sigmoidal because:a O2 binding to Hb increases the binding affinity of Hb for additional O2.b The pH of blood is near the pKa of histidine.c The pH of the bloodstream changes with changes in O2 concentration.d Hb’s O2-binding affinity changes with changes in pH.

Hemoglobin's affinity for oxygen increases as successive molecules of oxygen bind. As this limit is…

Answered: The O2-binding curve for Hemoglobin…

Human Physiology: From Cells to Systems (MindTap Course List)

9th Edition

ISBN:9781285866932

Author:Lauralee Sherwood

Publisher:Lauralee Sherwood

Chapter11: The Blood

Section: Chapter Questions

Problem 1SQE

See similar textbooks

Similar questions

Which of the following statements is false concerning the structure of hemoglobin? a. The binding of BPG stabilizes the T-state of Hb b. The R-state of Hb is favored under environments of high concentrations of O2 c. Hemoglobin's affinity for oxygen increases as protons ionize from the N-terminal tails d. Hemoglobin is stabilized in the low affinity state in the presence of high concentration of protons e. Hemoglobin favors the R-state in basic environments
Consider the Fe(Il) heme center in hemoglobin. Iron is colored orange and dioxygen is colored red. A. Circle the distal Histidine residue. B. What is the function of the distal Histidine residue? C. What keeps bound oxygen “bent", and not binding orthogonal to the plane of the porphyrin? D. What would happen to Fe(lI) if oxygen were to bind perpendicular (orthogonal) to the plane of the porphyrin? E. What happens to the structure of the porphyrin when oxygen dissociates from hemoglobin?
The graphs below show 02-binding curves of several proteins including myoglobin (Mb) and hemoglobin (Hb). If curve 3 (-) represents the 02 binding behavior of normal hemoglobin, which curve represents an 02-binding transporter with the same p50 as normal hemoglobin? 1.0- YO, 0.5 0.0 pO,(torr) O A. 1 B. 2 O C. 4 O D. 5 E. Both "2" and "4"
If there was a molecule that causes Hb to be more stable in the T state, this molecule would: a. Generally, raise the affinity of Hb for O2 b. Generally, lower the affinity of Hb for O2 c. Generally, cause Mb to favor the R state while Hb is in the T state d. Generally, cause Hb to dissociate into αβ dimers
Which of the following statement(s) is/are FALSE for hemoglobin? A Demonstrates positive cooperativity and can bind up to four O2 molecule. B It exhibits the 4 levels of protein structure. C It is a trimer with 2 α-helices and 1 β-sheet. D It is an allosteric protein.
In addition to O, binding, changes in other chemical conditions can result in hemoglobin changes. pH is one of those factors. It can be understood by reaction #1. Red blood cells have the enzyme Carbonic Anhydrase which catalyzes reaction #2. Using the two reactions explain how pH contributes to the transfer of O2 from the lungs to the tissues. H-Hb* + O2 Hb-O2 + H* Reaction #1 CO2(aq) + H2O= H* + HCO3 Reaction #2
One molecule of 2,3-BPG binds to one tetramer of hemoglobin in a central cavity of the hemoglobin molecule. Is the interaction between BPG and hemoglobin stronger or weaker than it would be if BPG bound to the surface of the protein instead? Explain your answer (hint: think about how these different situations affect the dielectric constant).
A point mutation in Hb diminishes hydrophobicity at the heme. Which of the following impacts would you predict? . Increased oxidation of Fe2+ and loss of O2 binding b. Decreased negative charges needed at the dimer/dimer interface to stabilize the T-state c. Decreased positive charges needed at the dimer/dimer interface to stabilize the T-state d. Shift the O2 binding curve of Hb to the left e. Decreased affinity for BPG in the T-state
One molecule of 2,3-BPG binds to one tetramer of hemoglobin in a central cavity of the hemoglobin molecule. Is the interaction between BPG and hemoglobin stronger or weaker than it would be if BPG bound to the surface of the protein instead? Explain your answer (hint: think about how these different situations affect the dielectric constant). (Please provide clear and sufficient explanation for the question, thank you!)
) Dr Merrick is so excited to know the affinity constant Kd values for O2 binding to mammoth OBP and elephant hemoglobin at pH=7, that he starts speculating about the kinetics of binding to O2. If the ka value of mammoth EHb-O2 complex was the same as the ka value of mammoth OBP-O2 complex, what would be the ratio between the kd values of these complexes? Explain your reasoning. Hint: we are looking for the ratio kd(EHb)/kd(OBP) at pH=7.
To study the chemical properties of the blood hemoglobin of a vertebrate, it might seem convenient to remove the hemoglobin from the red blood cells so that the hemoglobin is in simple aqueous solution. However, removing the hemoglobin from red blood cells often promptly alters its O2-binding characteristics. Why?
Which of the following best explains why fetal hemoglobin (HbF) has higher affinity for oxygen than HbA? a. HbF binds 2,3-bisphosphoglycerate with lower affinity b. One of the coordination positions of HbF is occupied by an Asp residue c. Oxygen binding is not cooperative in HbF d. The Fe-O bond is shorter in HbF e. The hemes of HbF and HbA have different structures

SEE MORE QUESTIONS

Recommended textbooks for you

Human Physiology: From Cells to Systems (MindTap …

Biology

ISBN:

9781285866932

Author:

Lauralee Sherwood

Publisher:

Cengage Learning