posted on 2024-03-05, 19:46authored byEhider
A. Polanco, Laura V. Opdam, Matthijs L. A. Hakkennes, Luuk Stringer, Anjali Pandit, Sylvestre Bonnet
Bovine carbonic anhydrase (BCA) is an enzyme that regulates
cellular
pH by catalyzing CO2 hydration. In this work, we used its
well-defined zinc-containing active site to host a series of four
sulfonamide-functionalized ruthenium-based water oxidation catalysts Ru1 to Ru4, thereby producing four BCA-Ru1 to BCA-Ru4 artificial metalloenzymes (ArMs). The four
ruthenium complexes differed either by the nature of the spectator
ligand (bda2– or tda2–) bound
to the catalytic center or by the length of the linker between the
axially ruthenium-bound pyridine moiety and the zinc-binding sulfonamide.
The two ArMs BCA-Ru1 and BCA-Ru2 were catalytically
active for photocatalytic water oxidation in aqueous solution in the
presence of [Ru(bpy)3](ClO4)2 as
a photosensitizer, Na2S2O8 as an
electron acceptor, and blue light (450 nm). The most active artificial
metalloenzyme, BCA-Ru1, could drive photocatalytic O2 production at particularly low ArM concentrations (5 μM),
yielding a turnover number (TON) of 348 and a turnover frequency (TOF)
of 9 min–1 that was 1 order of magnitude higher
than for the enzyme-free catalyst. A molecular dynamics study was
performed to model the interaction between the ruthenium catalyst
and the BCA protein. Overall, the protein scaffold modified
the second coordination sphere around the catalytic center, which
enhanced the activity and stability of two out of the four water oxidation
catalysts in aqueous solution, modifying their pH dependence and suppressing
the need for adding any organic solvents in solution. Altogether,
these results demonstrate how useful artificial metalloenzymes can
be for the making of artificial photosynthetic systems.