Liquid-phase chemistry: Graphene nanobubbles

X-Ray Photoelectron Spectroscopy (XPS) and X-Ray Absorption Spectroscopy (XAS) provide unique knowledge on the electronic structure and chemical properties of materials.

Unfortunately this information is scarce when investigating solid/liquid interfaces, chemical or photochemical reactions in ambient conditions because of the short electron inelastic mean free path (IMFP) that requires a vacuum environment, which poses serious limitation on the application of XPS and XAS to samples operating in atmosphere or in the presence of a solvent. One promising approach to enable the use of conventional electron spectroscopies is the use of thin membrane, such as graphene (Gr), which is transparent to both X-ray photons and photoelectrons. For these purposes, this work proposes an innovative system based on sealed Gr nanobubbles (GNBs) on a titanium dioxide TiO2 (100) rutile single crystal filled with the solution of interest during the fabrication stage (Figure 1a).

The formation of irregularly shaped vesicles with an average height of 6 nm and lateral size of a few hundreds of nanometers was proved by using a multi-technique approach involving Atomic Force Microscopy (AFM, see Figure 1b,c,d), Raman (Figure 1e) and synchrotron radiation spectroscopies (Figure 2), which have unequivocally demonstrated the presence of water inside the GNBs and the transition to a flat Gr layer after water evaporation by thermal heating up to 350 °C in ultra high vacuum (UHV).

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Chemistry at the protein-mineral interface

The nucleation site of iron mineral in human L ferritin revealed by anomalous -ray diffraction

Iron ions have crucial functions in every living organism being essential for cellular respiration, DNA synthesis, detoxification of exogenous compounds, just to provide a few examples. However, the redox properties of iron ions can also cause the occurrence of deleterious free-radicals. For these reasons, when unnecessary, iron must be kept in appropriate forms unable to cause damage. Nature evolved a special protein cage, called ferritin, consisting of 24 subunits arranged to form a hollow sphere with an internal diameter of about 80 Å where mineralized iron is stored, generally under the form of insoluble ferric oxides.

In mammals, two types of subunits build-up the 24-mer ferritins: the ‘heavy’ (H) and the ‘light’ (L). These subunits differ not only in molecular weight (21.2 kDa for H and 20.0 kDa for L) but, mainly, in function. The H subunit is able to catalyze the rapid oxidation of Fe2+ to Fe3+ followed by transfer in the storage cavity. On the contrary, the L-chain does not possess catalytic activity, but it is still able to mineralize ferric ions upon spontaneous oxidation by dioxygen of captured Fe2+. Despite the intensive research on ferritin chemistry, the mechanisms of iron oxidation and storage to form mineral nanoparticles inside the ferritin cavity are still to be fully established.

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