Improved thermoelectric properties of Aluminum Zinc Oxide (AZO) thin films deposited by radio frequency (RF) and pulsed Direct Current (DC) magnetron sputtering at room temperature are reported. In both techniques films were deposited using sintered and non-sintered targets produced from nano-powders. It is confirmed that both the Al doping concentration and film thickness control the thermoelectric, optical and structural properties of these films. Seebeck coefficients up to −134 μV K−1 and electrical conductivities up to 4 × 104 (Ω m)−1 lead to power factors up to 4 × 10−4 W mK−2, which is above the state-of-the-art for similar materials, almost by a factor of three. The thermoelectric I–V response of an optimized AZO element with a planar geometry was measured and a maximum power output of 2.3 nW, for a temperature gradient of 20 K near room temperature, was obtained. Moreover, the low thermal conductivity (<1.19 W mK−1) yields a ZT value above 0.1. This is an important result as it is at least three times higher than the ZT found in the literature for AZO, at room temperature, opening new doors for applications of this inexpensive, abundant and environmental friendly material, in a new era of thermoelectric devices.

By using monochromatic light the ability of semiconductor-free nanoporous carbons to convert the low-energy photons from the visible spectrum into chemical reactions (i.e. phenol photooxidation) is demonstrated. Data shows that the onset wavelength of the photochemical activity can be tuned by surface functionalization, with enhanced visible-light conversion upon introducing N-containing groups.

Arabinanase is a glycosyl hydrolase that is able to cleave the glycosidic bonds of α-1,5-L-arabinan, releasing arabino-oligosaccharides and L-arabinose. The enzyme has two domains, an N-terminal catalytic domain with a characteristic β-propeller fold and a C-terminal domain whose function is unknown. A calcium ion, located near the catalytic site, serves to stabilize the N-terminal domain, but it has also been proposed to play a key role in the enzyme mechanism. The present work describes the structure of an inactive mutant of the wild-type enzyme (H318Q) and in which the calcium ion has been adventitiously replaced by nickel. These structural studies, together with functional and modelling studies, clearly support the role of the calcium ion in the overall reaction mechanism.

Pulsed field gradient spin echo high resolution magic angle spinning nuclear magnetic resonance spectroscopy is a powerful technique to characterize confined biosystems. We used this approach to assess the diffusion of solvent and reaction species within sol–gel matrices differing in enzyme loading.