@article{FrascaMilanGuietetal.2013,
  author    = {Frasca, Stefano and Milan, Anabel Molero and Guiet, Amandine and Goebel, Caren and Perez-Caballero, Fernando and Stiba, Konstanze and Leimk{\"u}hler, Silke and Fischer, Anna and Wollenberger, Ursula},
  title     = {Bioelectrocatalysis at mesoporous antimony doped tin oxide electrodes-Electrochemical characterization and direct enzyme communication},
  series = {ELECTROCHIMICA ACTA},
  volume    = {110},
  journal   = {ELECTROCHIMICA ACTA},
  number    = {2},
  publisher = {PERGAMON-ELSEVIER SCIENCE LTD},
  address   = {OXFORD},
  issn      = {0013-4686},
  doi       = {10.1016/j.electacta.2013.03.144},
  pages     = {172 -- 180},
  year      = {2013},
  abstract  = {In this paper we report immobilization and bioelectrocatalysis of human sulfite oxidase (hSO) on nanostructured antimony doped tin oxide (ATO) thin film electrodes. Two types of ATO thin film electrodes were prepared via evaporation induced self-assembly of ATO nanoparticle sols. The use of a porogen results in different porosity and film thickness. Nevertheless both electrode types reveal similar quasi reversible electrochemical behavior for positive and negatively charged small mediators. Facile and durable immobilization of catalytically active enzyme in a direct electron transfer configuration was achieved without further chemical modification of the ATO surfaces. Interestingly, the binding of hSO onto the ATO surface seems to be not only of electrostatic nature, but also originates from a strong interaction between the histidine-tag of the enzyme and the supporting material. This is suggested from stable sulfite dependent bioelectrocatalytic signals at high ionic strength and imidazole desorption experiments. As such, ATO appears as a promising conductive platform for the immobilization of complex enzymes and their application in bioelectrocatalysis. (C) 2013 Elsevier Ltd. All rights reserved.},
  language  = {en}
}
@article{SivanesanKalaivaniFischeretal.2012,
  author    = {Sivanesan, Arumugam and Kalaivani, Govindasamy and Fischer, Anna and Stiba, Konstanze and Leimk{\"u}hler, Silke and Weidinger, Inez M.},
  title     = {Complementary surface-enhanced resonance raman Spectroscopic Biodetection of mixed protein solutions by Chitosan- and Silica-Coated Plasmon-Tuned Silver Nanoparticles},
  series = {Analytical chemistry},
  volume    = {84},
  journal   = {Analytical chemistry},
  number    = {13},
  publisher = {American Chemical Society},
  address   = {Washington},
  issn      = {0003-2700},
  doi       = {10.1021/ac301001a},
  pages     = {5759 -- 5764},
  year      = {2012},
  abstract  = {Silver nanoparticles with identical plasmonic properties but different surface functionalities are synthesized and tested as chemically selective surface-enhanced resonance Raman (SERR) amplifiers in a two-component protein solution. The surface plasmon resonances of the particles are tuned to 413 nm to match the molecular resonance of protein heme cofactors. Biocompatible functionalization of the nanoparticles with a thin film of chitosan yields selective SERR enhancement of the anionic protein cytochrome b(5), whereas functionalization with SiO2 amplifies only the spectra of the cationic protein cytochrome c. As a result, subsequent addition of the two differently functionalized particles yields complementary information on the same mixed protein sample solution. Finally, the applicability of chitosan-coated Ag nanoparticles for protein separation was tested by in situ resonance Raman spectroscopy.},
  language  = {en}
}