Exchange of Equatorial Ligands in Protein-bound Paddlewheel Ru25+ Complexes: New Insights form X-ray Crystallography and Quantum Chemistry
Abstract
Here we report the binding of the diruthenium complex [Ru2Cl(D-p-CNPhF)(O2CCH3)3]n (D-p-CNPhF– = N,N′-bis(4-cyanophenyl)formamidinate) to the model protein bovine pancreatic ribonuclease (RNase A), investigated for the first time by means of X-ray crystallography and Quantum Chemistry. The structure reveals that the compound binds an His side chain with the diruthenium core anchored to RNase A at the axial site, without significantly altering the overall protein structure. The protein binding to the diruthenium core is associated with the replacement of an acetate equatorial ligand by two water molecules. This species is expected to be highly reactive in the absence of the protein. Thus, the Ru2/RNase A structure here reported can be associated with the entatic state of the artificial metalloenzyme produced upon reaction of RNase A with [Ru2Cl(D-p-CNPhF)(O2CCH3)3]n. Quantum chemical investigations unveil the possible reaction mechanisms and help dissecting the role of the imidazole group axial ligands on the convenient replacement of equatorial acetate ligands by water molecules.
- This article is part of the themed collection: 2024 Inorganic Chemistry Frontiers HOT articles