In: Chemistry
To the nearest hundredths, what is the pH at the end of an enzyme-catalyzed reaction if it were carried out in a 0.1 M buffer initially at pH 6.65, and 0.006 M of acid (H+) was produced during the reaction? (The buffer used was a polyprotic acid of the general form: H3A; the three pKas of this polyprotic acid are 2.11, 6.65, and 11.33.)
The given pH = 6.65
The given pKa values of polyprotic acid (H3A): pKa1 = 2.11, pKa2 = 6.65 and pKa3 = 11.33
Here, pH = pKa2
i.e. The buffer mixture can be expressed as H2A-/HA2-
According to Henderson-Hasselbalch equation, we can write as shown below.
pH = pKa2 + Log[HA2-]/[H2A-]
Log[HA2-]/[H2A-] = 0 (since pH = pKa2)
i.e. [HA2-]/[H2A-] = 1
i.e. [HA2-] = [H2A-]
Given that the concentration of buffer = 0.1 M
i.e. [HA2-] + [H2A-] = 0.1
Therefore, [HA2-] = [H2A-] = 0.1/2, i.e. 0.05 M
Given that 0.006 M of acid (H+) was produced during the reaction.
i.e. [HA2-] = 0.05 - 0.006, i.e. 0.044 M (since HA2- is a base, which reacts with produced H+, as a result its concentration decreases)
and [H2A-] = 0.05 + 0.006, i.e. 0.056 M (since H2A- is an acid, which adds up to the produced H+, as a result its concentration increases)
Rewrite the Henderson-Hasselbalch equation: pH = pKa2 + Log[HA2-]/[H2A-]
i.e. pH = 6.65 + Log(0.044/0.056)
i.e. pH = 6.65 + (-0.105)
i.e. The pH at the end of an enzyme-catalyzed reaction = 6.545