A highly stable metal-organic framework, [{Fe3(ACTBA)2}X·6DEF]n (1; X = monoanion), based on trinuclear iron(iii) secondary building units connected by tetracarboxylates with an anthracene core, 2,6,9,10-tetrakis(p-carboxylatophenyl)anthracene (ACTBA), is reported. Depending on the direction of light polarisation, crystals of 1 exhibit anisotropic optical properties with birefringence Δn = 0.3 (λ = 590 nm).

The deposition of in-situ formed gold nanoparticles at the liquid/liquid (L/L) interface is studied by means of thin-organic-film-modified electrodes (TFE). The degree of ordering and aggregation of gold nanoparticles can be tuned by adding a lipophilic and hydrophilic thiol in the organic and aqueous phase, respectively. The ordered thiol-anchored gold nanoparticles exhibit pronounced catalytic effect toward electron-transfer reactions across the L/L interface.

A coupled electron-ion transfer reaction at thin organic-film-modified electrodes (TFE) is studied in the presence of glucose oxidase (GOx) under voltammetric conditions. TFE consists of a graphite electrode modified with a nitrobenzene solution of decamethylferrocene (DMFC) as a redox mediator and tetrabuthylammonium perchlorate as an organic-supporting electrolyte, in contact with aqueous buffer solutions containing percholarte ions and GOx. The redox turnover of DMFC coupled with perchlorate transfer across water|nitrobenzene interface composes the coupled electronion transfer reaction. Glucose oxidase strongly adsorbs at the liquid|liquid interface affecting the coupled electron-ion transfer reaction by reducing the surface area of the liquid interface, prompting coadsorption of the transferring ion and lowering down slightly the rate of the ion transfer reaction. Although the enzyme exists as a polyvalent anion over the pH interval from 5.6 to 7, it does not participate directly in the ionic current across the liquid interface and percholrate remains the main transferring ion. Raman spectroscopic data, together with the voltammetric data collected by three-phase droplet electrodes, indicate that the adsorption of the enzyme does not depend either on the redox mediator (DMFC) or the organicsupporting electrolyte, while being driven by intrinsic interactions of the enzyme with the organic solvent. The overall electrochemical mechanism is mathematically modeled by considering linear adsorption isotherm of the transferring ion, semi-infinite mass transfer regime, and phenomenological second-order kinetic model.