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In a previous paper, we presented an updated magnetic field map for the chemically peculiar star alpha(2) CVn using ESPaDOnS and Narval time-resolved high-resolution Stokes IQUV spectra. In this paper, we focus on mapping various chemical element distributions on the surface of alpha(2) CVn. With the new magnetic field map and new chemical abundance distributions, we can investigate the interplay between the chemical abundance structures and the magnetic field topology on the surface of alpha(2) CVn. Previous attempts at chemical abundance mapping of alpha(2) CVn relied on lower resolution data. With our high-resolution (R = 65 000) data set, we present nine chemical abundance maps for the elements O, Si, Cl, Ti, Cr, Fe, Pr, Nd and Eu. We also derive an updated magnetic field map from Fe and Cr lines in Stokes IQUV and O and Cl in Stokes IV. These new maps are inferred from line profiles in Stokes IV using the magnetic Doppler imaging code INVERS10. We examine these new chemical maps and investigate correlations with the magnetic topology of alpha(2) CVn. We show that chemical abundance distributions vary between elements, with two distinct groups of elements; one accumulates close to the negative part of the radial field, whilst the other group shows higher abundances located where the radial magnetic field is of the order of 2 kG regardless of the polarity of the radial field component. We compare our results with previous works which have mapped chemical abundance structures of Ap stars. With the exception of Cr and Fe, we find no clear trend between what we reconstruct and other mapping results. We also find a lack of agreement with theoretical predictions. This suggests that there is a gap in our theoretical understanding of the formation of horizontal chemical abundance structures and the connection to the magnetic field in Ap stars.

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A small fraction of intermediate-mass main sequence (A and B type) stars have strong, organised magnetic fields. The large majority of such stars, however, show no evidence for magnetic fields, even when observed with very high precision. In this paper we describe a simple model, motivated by qualitatively new observational results, that provides a natural physical explanation for the small fraction of observed magnetic stars.

Historically, the magnetic field geometries of the chemically peculiar Ap stars were modelled in the context of a simple dipole field. However, with the acquisition of increasingly sophisticated diagnostic data, it has become clear that the large-scale field topologies exhibit important departures from this simple model. Recently, new high-resolution circular and linear polarisation spectroscopy has even hinted at the presence of strong, small-scale field structures, which were completely unexpected based on earlier modelling. This project investigates the detailed structure of these strong fossil magnetic fields, in particular the large-scale field geometry, as well as small scale magnetic structures, by mapping the magnetic and chemical surface structure of a selected sample of Ap stars. These maps will be used to investigate the relationship between the local field vector and local surface chemistry, looking for the influence the field may have on the various chemical transport mechanisms (i.e., diffusion, convection and mass loss). This will lead to better constraints on the origin and evolution, as well as refining the magnetic field model for Ap stars. Mapping will be performed using high resolution and signal-to-noise ratio time-series of spectra in both circular and linear polarisation obtained using the new-generation ESPaDOnS (CFHT, Mauna Kea, Hawaii) and NARVAL spectropolarimeters (Pic du Midi Observatory). With these data we will perform tomographic inversion of Doppler-broadened Stokes IQUV Zeeman profiles of a large variety of spectral lines using the INVERS10 magnetic Doppler imaging code, simultaneously recovering the detailed surface maps of the vector magnetic field and chemical abundances.

Porphyrin-sensitized photo-oxidation of bovine serum albumin results in oxidation at specific sites to produce protein radical species: at the Cys-34 residue (to give a thiyl radical) and at one or both tryptophan residues (Trp-134 and Trp-214) to give tertiary carbon-centered radicals and cause disruption of the indole ring system. This study shows that these photo-oxidation processes also consume oxygen and give rise to hydrogen peroxide, protein hydroperoxides, and carbonyl functions. The yield of hydrogen peroxide, protein hydroperoxides, and carbonyl functions is shown to be dependent on illumination time, the nature of the sensitizer, and the concentration of oxygen; the yield of hydroperoxides can also be markedly diminished by the presence of a spin trap which reacts with the initial protein radicals. The mechanism of formation of the protein hydroperoxides is suggested to be primarily through type I processes (i.e., independent of singlet oxygen), while type II (singlet oxygen) mechanisms may play a significant role in protein carbonyl formation. Reaction of the protein hydroperoxide species with metal ion complexes is shown to produce further protein-derived radicals which are predominantly present on amino acid side chains.

Porphyrin-sensitized photoxidation of bovine serum albumin (BSA) results in oxidation of the protein at (at least) two different, specific sites: the Cys-34 residue giving rise to a thiyl radical (RS.); and one or both of the tryptophan residues (Trp-134 and Trp-214) resulting in the formation of tertiary carbon-centred radicals and disruption of the tryptophan ring system. In the case of porphyrins such as hematoporphyrin, which bind at specific sites on BSA, these species appear to arise via long-range transfer of damage within the protein structure, as the binding site is some distance from the ultimate site of radical formation. This transfer of damage is shown to depend on a number of factors including the conformation of the protein, the presence of blocking groups and pH. Alteration of the protein conformation results in radical formation at additional (or alternative) sites, as does blocking of the preferred loci of radical formation. The formation of these thiyl and tryptophan-derived radicals does not lead to significant aggregation or fragmentation of the protein, though it does result in a dramatic enhancement in the susceptibility of the oxidised protein to proteolytic degradation by a range of proteases. The generation of protein-derived radicals also results in an enhancement of photobleaching of the porphyrin, suggesting that protein radical generation is linked to porphyrin photooxidation.