@article{SarauliRiedelWettsteinetal.2012,
  author    = {Sarauli, David and Riedel, Marc and Wettstein, Christoph and Hahn, Robert and Stiba, Konstanze and Wollenberger, Ursula and Leimk{\"u}hler, Silke and Schmuki, Patrik and Lisdat, Fred},
  title     = {Semimetallic TiO2 nanotubes new interfaces for bioelectrochemical enzymatic catalysis},
  series = {Journal of materials chemistry},
  volume    = {22},
  journal   = {Journal of materials chemistry},
  number    = {11},
  publisher = {Royal Society of Chemistry},
  address   = {Cambridge},
  issn      = {0959-9428},
  doi       = {10.1039/c2jm16427b},
  pages     = {4615 -- 4618},
  year      = {2012},
  abstract  = {Different self-organized TiO2 nanotube structures are shown to represent new interfaces for the achievement of bioelectrochemical enzymatic catalysis involving redox proteins and enzymes without further surface modification or the presence of mediators.},
  language  = {en}
}
@phdthesis{Wettstein2015,
  author    = {Wettstein, Christoph},
  title     = {Cytochrome c-DNA and cytochrome c-enzyme interactions for the construction of analytical signal chains},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-78367},
  school      = {Universit{\"a}t Potsdam},
  pages     = {120},
  year      = {2015},
  abstract  = {Electron transfer (ET) reactions play a crucial role in the metabolic pathways of all organisms. In biotechnological approaches, the redox properties of the protein cytochrome c (cyt c), which acts as an electron shuttle in the respiratory chain, was utilized to engineer ET chains on electrode surfaces. With the help of the biopolymer DNA, the redox protein assembles into electro active multilayer (ML) systems, providing a biocompatible matrix for the entrapment of proteins. In this study the characteristics of the cyt c and DNA interaction were defined on the molecular level for the first time and the binding sites of DNA on cyt c were identified. Persistent cyt c/DNA complexes were formed in solution under the assembly conditions of ML architectures, i.e. pH 5.0 and low ionic strength. At pH 7.0, no agglomerates were formed, permitting the characterization of the NMR spectroscopy. Using transverse relaxation-optimized spectroscopy (TROSY)-heteronuclear single quantum coherence (HSQC) experiments, DNAs' binding sites on the protein were identified. In particular, negatively charged AA residues, which are known interaction sites in cyt c/protein binding were identified as the main contact points of cyt c and DNA. Moreover, the sophisticated task of arranging proteins on electrode surfaces to create functional ET chains was addressed. Therefore, two different enzyme types, the flavin dependent fructose dehydrogenase (FDH) and the pyrroloquinoline quinone dependent glucose dehydrogenase (PQQ-GDH), were tested as reaction partners of freely diffusing cyt c and cyt c immobilized on electrodes in mono- and MLs. The characterisation of the ET processes was performed by means of electrochemistry and the protein deposition was monitored by microgravimetric measurements. FDH and PQQ-GDH were found to be generally suitable for combination with the cyt c/DNA ML system, since both enzymes interact with cyt c in solution and in the immobilized state. The immobilization of FDH and cyt c was achieved with the enzyme on top of a cyt c monolayer electrode without the help of a polyelectrolyte. Combining FDH with the cyt c/DNA ML system did not succeed, yet. However, the basic conditions for this protein-protein interaction were defined. PQQ-GDH was successfully coupled with the ML system, demonstrating that that the cyt c/DNA ML system provides a suitable interface for enzymes and that the creation of signal chains, based on the idea of co-immobilized proteins is feasible. Future work may be directed to the investigation of cyt c/DNA interaction under the precise conditions of ML assembly. Therefore, solid state NMR or X-ray crystallography may be required. Based on the results of this study, the combination of FDH with the ML system should be addressed. Moreover, alternative types of enzymes may be tested as catalytic component of the ML assembly, aiming on the development of innovative biosensor applications.},
  language  = {en}
}
@article{WettsteinKanoSchaeferetal.2016,
  author    = {Wettstein, Christoph and Kano, Kenji and Schaefer, Daniel and Wollenberger, Ursula and Lisdat, Fred},
  title     = {Interaction of Flavin-Dependent Fructose Dehydrogenase with Cytochrome c as Basis for the Construction of Biomacromolecular Architectures on Electrodes},
  series = {Analytical chemistry},
  volume    = {88},
  journal   = {Analytical chemistry},
  publisher = {American Chemical Society},
  address   = {Washington},
  issn      = {0003-2700},
  doi       = {10.1021/acs.analchem.6b00815},
  pages     = {6382 -- 6389},
  year      = {2016},
  abstract  = {The creation of electron transfer (ET) chains based on the defined arrangement of enzymes and redox proteins on electrode surfaces represents an interesting approach within the field of bioelectrocatalysis. In this study, we investigated the ET reaction of the flavin-dependent enzyme fructose dehydrogenase (FDH) with the redox protein cytochrome c (cyt c). Two different pH optima were found for the reaction in acidic and neutral solutions. When cyt c was adsorbed on an electrode surface while the enzyme remained in solution, ET proceeded efficiently in media of neutral pH. Interprotein ET was also observed in acidic media; however, it appeared to be less efficient. These findings suggest that two different ET pathways between the enzyme and cyt c may occur. Moreover, cyt c and FDH were immobilized in multiple layers on an electrode surface by means of another biomacromolecule: DNA (double stranded) using the layer -by -layer technique. The biprotein multilayer architecture showed a catalytic response in dependence on the fructose concentration, indicating that the ET reaction between both proteins is feasible even in the immobilized state. The electrode showed a defined response to fructose and a good storage stability. Our results contribute to the better understanding of the ET reaction between FDH and cyt c and provide the basis for the creation of all-biomolecule based fructose sensors the sensitivity of which can be controlled by the layer preparation.},
  language  = {en}
}