Metallic elements are essential components of many important enzymes operating
within our bodies. Carbonic anhydrase, which contains \(\mathrm{Zn}^{2+}\) in
its active site, is responsible for rapidly interconverting dissolved
\(\mathrm{CO}_{2}\) and bicarbonate ion, \(\mathrm{HCO}_{3}^{-}\). The zinc in
carbonic anhydrase is tetrahedrally coordinated by three neutral
nitrogencontaining groups and a water molecule. The coordinated water molecule
has a \(\mathrm{p} K_{a}\) of \(7.5,\) which is crucial for the enzyme's activity.
(a) Draw the active site geometry for the \(\mathrm{Zn}(\mathrm{II})\) center in
carbonic anhydrase, just writing "N" for the three neutral nitrogen ligands
from the protein.
(b) Compare the \(\mathrm{p} K_{a}\) of carbonic anhydrase's active site with
that of pure water; which species is more acidic?
(c) When the coordinated water to the \(\mathrm{Zn}(\mathrm{II})\) center in
carbonic anhydrase is deprotonated, what ligands are bound to the
\(\mathrm{Zn}(\mathrm{II})\) center? Assume the three nitrogen ligands are
unaffected. \((\mathbf{d})\) The \(\mathrm{p} K_{a}\) of
\(\left[\mathrm{Zn}\left(\mathrm{H}_{2} \mathrm{O}\right)_{6}\right]^{2+}\) is
\(10 .\) Suggest an explanation for the difference between this \(\mathrm{p}
K_{a}\) and that of carbonic anhydrase. (e) Would you expect carbonic anhydrase
to have a deep color, like hemoglobin and other metal-ion-containing proteins
do? Explain.