Comparison of Intra- vs Intermolecular Long-Range Electron Transfer in Crystals of Ruthenium-Modified Azurin

Selective metal-ion incorporation and ligand substitution are employed to control whether electrons tunnel over intra- or intermolecular separations in crystals of P. aeruginosa azurin modified with Ru−polypyridine complexes. Cu1+-to-Ru3+ electron transfer (ET) across a specific protein−protein interface in the crystal lattice has a time constant 5−10 times longer than ET between the same donor and acceptor within a single protein (τET = 5 vs 0.5−1.0 μs). Slower intermolecular ET agrees well with a longer distance between redox centers across the inter-protein (18.9 Å) compared to the intra-protein separation (17.0 Å) and indicates that the closest donor/acceptor pair dominates crystal ET. Lowering the crystal pH accelerates inter-protein ET (τET = 1.0 μs) but not intra-protein ET. Faster inter-protein ET likely results from a pH-induced peptide bond flip that perturbs hydrogen bonding in the path between Ru and Cu centers on adjacent molecules.