Atomic layer deposition of HfO2 on graphene from HfCl4 and H20

Atomic layer deposition of ultrathin HfO2 on unmodified graphene from HfCl4 and H2O was investigated. Surface RMS roughness down to 0.5 nm was obtained for amorphous, 30 nm thick hafnia film grown at 180 degrees C. HfO2 was deposited also in a two-step temperature process where the initial growth of about 1 nm at 170 degrees C was continued up to 10-30 nm at 300 degrees C. This process yielded uniform, monoclinic HfO2 films with RMS roughness of 1.7 nm for 10-12 nm thick films and 2.5 nm for 30 nm thick films. Raman spectroscopy studies revealed that the deposition process caused compressive biaxial strain in graphene whereas no extra defects were generated. An 11 nm thick HfO2 film deposited onto bilayer graphene reduced the electron mobility by less than 10% at the Dirac point and by 30-40% far away from it.Comment: 4 figures, accepted by CEJ

Plasmon Enhancement of Fluorescence in Single Light-Harvesting Complexes from em Amphidinium carterae

We show that single peridinin-chlorophyll a-protein light-harvesting complexes from dinoflagellate Amphidinium carterae placed near to silver nanoparticles show strongly enhanced fluorescence emission. Single molecule spectroscopy experiments performed at room temperature point toward an enhancement of more than an order of magnitude for optimal conditions. Irrespective of the enhancement, we observe no effect of the metal nanoparticle on the fluorescence emission energy of the complex. This result provides a way to control the optical properties of biomolecules via plasmon excitations in metal nanoparticles

Conservation of spin polarization during triplet-triplet energy transfer in reconstituted peridinin-chlorophyll-protein complexes

Peridinin-chlorophyll-protein (PCP) complexes, where the N-terminal domain of native PCP from Amphidinium carterae has been reconstituted with different chlorophyll (Chl) species, have been investigated by time-resolved EPR in order to elucidate the details of the triplet-triplet energy transfer (TTET) mechanism. This spectroscopic approach exploits the concept of spin conservation during TTET, which leads to recognizable spin-polarization effects in the observed time-resolved EPR spectra. The spin polarization produced at the acceptor site (peridinin) depends on the initial polarization of the donor (chlorophyll) and on the relative geometric arrangement of the donor-acceptor spin axes. A variation of the donor triplet state properties in terms of population probabilities or triplet spin axis directions, as produced by replacement of chlorophyll a (Chl a) with non-native chlorophyll species (ZnChl a and BacterioChl a) in the reconstituted complexes, is unambiguously reflected in the polarization pattern of the carotenoid triplet state. For the first time, in the present investigation spin-polarization conservation has been shown to occur among natural cofactors in protein complexes during the TTET process. Proving the validity of the assumption of spin conservation adopted in the EPR spectral analysis, the results reinforce the hypothesis that in PCP proteins peridinin 614, according to X-ray nomenclature (Hofmann, E.; et al. Science1996, 272, 1788-1791), is the carotenoid of election in the photoprotection mechanism based on TTET.10 page(s