Light-Induced Charge Separation in Densely Packed Donor–Acceptor Coordination Cages

Photon-powered charge separation is achieved in a supramolecular architecture based on the dense packing of functional building blocks. Therefore, self-assembled dimers of interpenetrated coordination cages consisting of redoxactive chromophors were synthesized in a single assembly step starting from easily accessible ligands and Pd­(II) cations. Two backbones consisting of electron rich phenothiazine (PTZ) and electron deficient anthraquinone (ANQ) were used to assemble either homo-octameric or mixed-ligand double cages. The electrochemical and spectroscopic properties of the pure cages, mixtures of donor and acceptor cages and the mixed-ligand cages were compared by steady-state UV–vis and transient absorption spectroscopy, supported by cyclic voltammetry and spectroelectrochemistry. Only the mixed-ligand cages, allowing close intra-assembly communication between the donors and acceptors, showed the evolution of characteristic PTZ radical cation and ANQ radical anion features upon excitation in the transient spectra. In contrast, excitation of the mixtures of the homo-octameric donor and acceptor cages in solution did not lead to any signs of electron transfer. Densely packed photo- and redox-functional self-assemblies promise molecular-level control over the morphology of the charge separation layer in future photovoltaic applications

Properties of Site-Specifically Incorporated 3‑Aminotyrosine in Proteins To Study Redox-Active Tyrosines: <i>Escherichia coli</i> Ribonucleotide Reductase as a Paradigm

3-Aminotyrosine (NH₂Y) has been a useful probe to study the role of redox active tyrosines in enzymes. This report describes properties of NH₂Y of key importance for its application in mechanistic studies. By combining the tRNA/NH₂Y-RS suppression technology with a model protein tailored for amino acid redox studies (α₃X, X = NH₂Y), the formal reduction potential of NH₂Y₃₂(O^•/OH) (<i><i>E</i>°′</i> = 395 ± 7 mV at pH 7.08 ± 0.05) could be determined using protein film voltammetry. We find that the Δ<i><i>E</i>°′</i> between NH₂Y₃₂(O^•/OH) and Y₃₂(O^•/OH) when measured under reversible conditions is ∼300–400 mV larger than earlier estimates based on irreversible voltammograms obtained on aqueous NH₂Y and Y. We have also generated D₆-NH₂Y₇₃₁-α2 of ribonucleotide reductase (RNR), which when incubated with β2/CDP/ATP generates the D₆-NH₂Y₇₃₁^•-α2/β2 complex. By multifrequency electron paramagnetic resonance (35, 94, and 263 GHz) and 34 GHz ¹H ENDOR spectroscopies, we determined the hyperfine coupling (hfc) constants of the amino protons that establish RNH₂^• planarity and thus minimal perturbation of the reduction potential by the protein environment. The amount of Y in the isolated NH₂Y-RNR incorporated by infidelity of the tRNA/NH₂Y-RS pair was determined by a generally useful LC-MS method. This information is essential to the utility of this NH₂Y probe to study any protein of interest and is employed to address our previously reported activity associated with NH₂Y-substituted RNRs