Which occurs when a hemoglobin molecule binds oxygen in the lungs? a The first O2 molecule binds more easily than the last O2 molecule. b Each heme group can reversibly bind four O2 molecules simultaneously. c Salt bridges between subunits break as the first O2 binds. d Cooperative binding of O2 causes the four subunits to dissociate e An iron atom is removed from a porphyrin group.

Which occurs when a hemoglobin molecule binds oxygen in the lungs? a The first O2 molecule binds more easily than the last O2 molecule. b Each heme group can reversibly bind four O2 molecules simultaneously. c Salt bridges between subunits break as the first O2 binds. d Cooperative binding of O2 causes the four subunits to dissociate e An iron atom is removed from a porphyrin group.

Human Biology (MindTap Course List)

11th Edition

ISBN:9781305112100

Author:Cecie Starr, Beverly McMillan

Publisher:Cecie Starr, Beverly McMillan

Chapter8: Blood

Section: Chapter Questions

Problem 3RQ

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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?
Which statement describes hemoglobin's cooperativity? A. When tetrameric hemoglobin binds one molecule of O2, its shape changes to make it bind more readily to a second molecule of O2. B. When tetrameric hemoglobin binds one molecule of O2 its shape changes, which prevents binding of any more O2 molecules. C. When oxygen is present in the blood, the shape of hemoglobin changes to allow oxygen to bind to it. D. When the oxygen concentration in blood decreases, then hemoglobin changes its shape to retain oxygen more readily. E. None of the above answer choices correctly describes cooperativity.
How does hemoglobin bind O2 cooperatively? A. The binding of one molecule of O2 to one subunit of hemoglobin enhances the assembly of other subunits to form a complete hemoglobin protein. B. The binding of one molecule of O2 to one hemoglobin protein enhances the binding of a molecule of O2 to a different hemoglobin protein. C. The binding of one molecule of O2 to one subunit of hemoglobin enhances the affinity of the same subunit for more molecules of O2. D. The binding of one molecule of O2 to one subunit of hemoglobin enhances the affinity of other subunits for O2.
Which molecule has the greatest ability to stabilize the deoxy state of hemoglobin? Select one: a. all have equal ability b. ВPG C. CO d. H e. Co2
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
The Hemoglobin subunits use a histidine amino acid to hold on to the heme group needed to chelate oxygen. You discover a new mutation in the Alpha-globin gene that causes it to code for a glycine instead of a histidine. These amino acids are very chemically different. Hypothesize how this mutation might affect oxygen transport.
Which of the following is not a feature of the Bohr effect? Group of answer choices A. a histidine protonates at an elevated pH value than free imidazole B. ion-pair formation increases proton affinity to hemoglobin C. noncovalent carbon dioxide binding assists oxygen unloading in tissues D. new salt bridges are formed from the covalent attachment of carbon dioxide E. the covalent attachment of carbon dioxide to hemoglobin causes a pH drop
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.
Which of the following statements is INCORRECT about how the components of hemoglobin are recycled? a. Iron ions are either stored in a phagocytic cell or circulate in the blood, bound to transferrin (a plasma protein). b. Each heme is stripped of its iron and converted to bilirubin, then excreted in bile. c. The alpha and beta chains are released into the bloodstream for use by other cells. d. Hemoglobin can be recycled only if phagocytized by macrophages.
What is the name of the molecule when glucose is bound to hemoglobin? a. Glycohemoglobin b. Beta cell c. Glycosylated molecule d. RBC complex
What is the primary role of the B-vtiamins? A. Involved in red blood cell production B. Assist immune function C. Maintian acid-base balance D. Act as conenzymes for energy metabolism
Which reaction is catalyzed by carbonic anhydrase?a. HPO42-+H+ ↔ H2PO4-b. CO2 + H2O ↔ H2CO3c. H2PO4 − +OH− ↔ HPO4 2 − +H2O

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a		The first O₂ molecule binds more easily than the last O₂ molecule.
b		Each heme group can reversibly bind four O₂ molecules simultaneously.
c		Salt bridges between subunits break as the first O₂ binds.
d		Cooperative binding of O₂ causes the four subunits to dissociate
e		An iron atom is removed from a porphyrin group.