Stimuli-responsive structural reorganizations play an important role in biological processes, often in combination with kinetic control scenarios. In supramolecular mimics of such systems, light has been established as the perfect external trigger. Here, we report on the light-driven structural rearrangement of a small, self-assembled Pd3L6 ring based on photochromic dithienylethene (DTE) ligands into a rhombicuboctahedral Pd24L48 sphere measuring about 6.4 nm across. When the wavelength is changed, this interconversion can be fully reversed, as confirmed by NMR and UV/Vis spectroscopy as well as mass spectrometry. The sphere was visualized by AFM, TEM, and GISAXS measurements. Due to dissimilarities in the photoswitch conformations, the interconversion rates between the two assemblies are drastically different in the two directions.

The first transition metal-free catalyzed direct C–H arylation of a variety of heteroarenes at room temperature has been reported using a phenalenyl-based radical without employing any photoactivation step.

In recent years, merging different types of catalysis in a single pot has drawn considerable attention and these catalytic processes have mainly relied upon metals. However, development of a completely metal free approach integrating organic redox and organic Lewis acidic property into a single system has been missing in the current literature. This study establishes that a redox active phenalenyl cation can activate one of the substrates by single electron transfer process while the same can activate the other substrate by a donor-acceptor type interaction using its Lewis acidity. This approach has successfully achieved light and metal-free catalytic C-H functionalization of unactivated arenes at ambient temperature (39 entries, including core moiety of a top-selling molecule boscalid), an economically attractive alternative to the rare metal-based multicatalysts process. A tandem approach involving trapping of reaction intermediates, spectroscopy along with density functional theory calculations unravels the dual role of phenalenyl cation.

This study investigates the mechanism of O–O bond cleavage in heme-copper oxidase (HCO) enzymes, combining experimental and computational insights from enzyme intermediates and synthetic models. It is determined that HCOs undergo a proton-initiated O–O cleavage mechanism where a single water molecule in the active site enables proton transfer (PT) from the cross-linked tyrosine to a peroxo ligand bridging the heme FeIII and CuII, and multiple H-bonding interactions lower the tyrosine pKa. Due to sterics within the active site, the proton must either transfer initially to the O(Fe) (a high-energy intermediate), or from another residue over a ~10 Å distance to reach the O(Cu) atom directly. While the distance between the H+ donor (Tyr) and acceptor (O(Cu)) results in a barrier to PT, this separation is critical for the low barrier to O–O cleavage as it enhances backbonding from Fe into the O–O σ* orbital. Thus, PT from Tyr precedes O–O elongation and is rate-limiting, consistent with available kinetic data. The electron transfers from tyrosinate after the barrier via a superexchange pathway provided by the cross-link, generating intermediate PM. PM is evaluated using available experimental data. The geometric structure contains an FeIV=O that is H-bonded to the CuII-OH. The electronic structure is a singlet, where the FeIV and CuII are antiferromagnetically coupled through the H-bond between the oxo(Fe) and hydroxo(Cu) ligands, while the CuII and Tyr• are ferromagnetically coupled due their delocalization into orthogonal magnetic orbitals on the cross-linked His residue. These findings provide critical insights into the mechanism of efficient O2 reduction in HCOs, and the nature of the PM intermediate that couples this reaction to proton pumping.

Unraveling the mechanism of ceruloplasmin (Cp) is fundamentally important towards understanding the pathogenesis of metal-mediated diseases and metal neurotoxicity. Here we report that Cl−, the most abundant anion in blood plasma, is a key component of Cp catalysis. Based on detailed spectroscopic analyses, Cl− preferentially interacts with the partially reduced trinuclear Cu cluster (TNC) in Cp under physiological conditions and shifts the electron equilibrium distribution among the two redox active type 1 (T1) Cu sites and the TNC. This shift in potential enables the intramolecular electron transfer (IET) from the T1 Cu to the native intermediate (NI) and accelerates the IET from the T1 Cu to the TNC, resulting in faster turnover in Cp catalysis.