Competitive Valerate Binding Enables RuO-Mediated Butene Electrosynthesis in Water.

The (non)-Kolbe oxidation of valeric acid, sourced from a hydrolysis product of cellulose, provides a sustainable synthetic route to access value-added products, such as butene. An essential mechanistic step preceding product formation involves the oxidative and decarboxylative cleavage of a C-C bond. Yet, the role of the electrode surface in mediating this oxidative step remains an open question: the electron transfer can occur either via an inner-sphere or outer-sphere mechanism.

Catalytic, Spectroscopic, and Theoretical Studies of FeS-Based Coordination Polymers as Heterogenous Coupled Proton-Electron Transfer Mediators for Electrocatalysis.

Iron-sulfur clusters play essential roles in biological systems, and thus synthetic [FeS] clusters have been an area of active research. Recent studies have demonstrated that soluble [FeS] clusters can serve as net H atom transfer mediators, improving the activity and selectivity of a homogeneous Mn CO reduction catalyst. Here, we demonstrate that incorporating these [FeS] clusters into a coordination polymer enables heterogeneous H atom transfer from an electrode surface to a Mn complex dissolved in solution.

Flanking Domains Modulate α-Synuclein Monomer Structure: A Molecular Dynamics Domain Deletion Study.

Aggregates of misfolded α-synuclein proteins (asyn) are key markers of Parkinson's disease. Asyn proteins have three domains: an N-terminal domain, a hydrophobic NAC core implicated in aggregation, and a proline-rich C-terminal domain. Proteins with truncated C-terminal domains are known to be prone to aggregation and suggest that studying domain-domain interactions in asyn monomers could help elucidate the role of the flanking domains in modulating protein structure.