25. 2,3-bisphosphoglyceric acid decreases Hemoglobin’s affinity for oxygen by: A

Question

25. 2,3-bisphosphoglyceric acid decreases Hemoglobin’s affinity for oxygen by:

A. binding to an Hemoglobin dimer.

B. binding to the subunits of Hemoglobin in the high affinity R state.

C. binding to the subunits of Hemoglobin in the low affinity T state.

D. binding to 5 positively charged amino acid R-groups of the 2 -subunits.

E. binding of 5 negatively charged amino acid R-groups of the 2 -subunits.

26. The effect of pH on the binding of oxygen to hemoglobin results in:

A. an affinity decrease with lower H+ concentration, i.e., increasing pH.

B. decreasing protonation of -chains His 146 with decreasing pH (i.e., higher

H+ concentration) which stabilizes the T state conformation of Hemoglobin.

C. decreasing protonation of -chains His 146 with decreasing pH (i.e., higher

H+ concentration) which stabilizes the R state conformation of Hemoglobin.

D. increasing protonation of -chains His 146 with decreasing pH (i.e., higher

H+ concentration) which stabilizes the T state conformation of Hemoglobin.

E. increasing protonation of -chains His 146 with decreasing pH (i.e., higher H+

concentration) which stabilizes the R state conformation of Hemoglobi

Explanation / Answer

25). C. binding to the subunits of Hemoglobin in the low affinity T state.

26).

D. increasing protonation of -chains His 146 with decreasing pH (i.e., higher

H+ concentration) which stabilizes the T state conformation of Hemoglobin.

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