@article{XieTangWollenbergeretal.1997,
  author    = {Xie, B. and Tang, X. and Wollenberger, Ursula and Johansson, G. and Gorton, Lo and Scheller, Frieder W. and Danielsson, B.},
  title     = {Hybrid biosensor for simultaneous electrochemical and thermal detection},
  year      = {1997},
  language  = {en}
}
@article{WuWollenbergerHofrichteretal.2011,
  author    = {Wu, Yunhua and Wollenberger, Ursula and Hofrichter, Martin and Ullrich, Rene and Scheibner, Katrin and Scheller, Frieder W.},
  title     = {Direct electron transfer of Agrocybe aegerita peroxygenase at electrodes modified with chitosan-capped Au nanoparticles and its bioelectrocatalysis to aniline},
  series = {Sensors and actuators : B, Chemical},
  volume    = {160},
  journal   = {Sensors and actuators : B, Chemical},
  number    = {1},
  publisher = {Elsevier},
  address   = {Lausanne},
  issn      = {0925-4005},
  doi       = {10.1016/j.snb.2011.09.090},
  pages     = {1419 -- 1426},
  year      = {2011},
  abstract  = {Three different sizes of chitosan-capped Au nanoparticles were synthesized and were used to incorporate Agrocybe aegerita peroxygenase (AaeAPO) onto the surface of glassy carbon electrode. The direct electron transfer of AaeAPO was achieved in all films. The highest amount of electroactive enzyme and highest electron transfer rate constant k(s) of AaeAPO were obtained in the film with the smallest size of chitosan-capped Au nanoparticles. In anaerobic solutions, quasi-reversible oxidation and reduction are obtained with a formal potential of -0.280V vs. Ag/AgCl 1 M KCl in 100 mM (pH 7.0) PBS at scan rate of 1 V s(-1). Bioelectrocatalytic reduction currents can be obtained with the AaeAPO-modified electrode on addition of hydrogen peroxide. This reaction was suppressed when sodium azide, an inhibitor of AaeAPO, was present. Furthermore, the peroxide-dependent conversion of aniline was characterized and it was found that a polymer product via p-aminophenol is formed. And the AaeAPO biosensor was applied to determine aniline and p-aminophenol.},
  language  = {en}
}
@article{WollenbergerSchubertPfeifferetal.1996,
  author    = {Wollenberger, Ursula and Schubert, Florian and Pfeiffer, Dorothea and Scheller, Frieder W.},
  title     = {Recycling sensors based on kinases : proceedings of Mosbach Symposion on Biochemical Technology},
  year      = {1996},
  language  = {en}
}
@article{WollenbergerSchubertPfeifferetal.1993,
  author    = {Wollenberger, Ursula and Schubert, Florian and Pfeiffer, Dorothea and Scheller, Frieder W.},
  title     = {Enhancing biosensor performance using multienzyme systems},
  year      = {1993},
  language  = {en}
}
@article{WollenbergerScheller1993,
  author    = {Wollenberger, Ursula and Scheller, Frieder W.},
  title     = {Enzyme activation for activator and enzyme activity measurement},
  year      = {1993},
  language  = {en}
}
@book{WollenbergerRennebergBieretal.2003,
  author    = {Wollenberger, Ursula and Renneberg, Reinhard and Bier, Frank Fabian and Scheller, Frieder W.},
  title     = {Analytische Biochemie : eine praktische Einf{\"u}hrung in das Messen mit Biomolek{\"u}len},
  publisher = {John Wiley \& Sons},
  address   = {Hoboken},
  isbn      = {3-527-30166-6},
  pages     = {222 S.},
  year      = {2003},
  language  = {de}
}
@article{WollenbergerNeumannScheller1998,
  author    = {Wollenberger, Ursula and Neumann, B. and Scheller, Frieder W.},
  title     = {Development of a biomimetic alkane sensor f},
  year      = {1998},
  language  = {en}
}
@article{WollenbergerNeumannScheller1993,
  author    = {Wollenberger, Ursula and Neumann, B. and Scheller, Frieder W.},
  title     = {Enzyme and microbial sensors for environmental Monitoring},
  year      = {1993},
  language  = {en}
}
@article{WollenbergerNeumannRiedeletal.1994,
  author    = {Wollenberger, Ursula and Neumann, B. and Riedel, K. and Scheller, Frieder W.},
  title     = {Enzyme and microbial sensors for phosphate, phenols, pesticides and peroxides},
  year      = {1994},
  language  = {en}
}
@article{WollenbergerNeumann1997,
  author    = {Wollenberger, Ursula and Neumann, B.},
  title     = {Quinoprotein glucose dehydrogenase modified carbon paste electrode for detection of phenolic compounds},
  year      = {1997},
  language  = {en}
}
@article{WollenbergerLisdatScheller1997,
  author    = {Wollenberger, Ursula and Lisdat, Fred and Scheller, Frieder W.},
  title     = {Enzymatic substrade recycling electrodes},
  year      = {1997},
  language  = {en}
}
@article{WollenbergerJung2001,
  author    = {Wollenberger, Ursula and Jung, Christiane},
  title     = {Cytochrom P450-Elektrochemie},
  year      = {2001},
  language  = {de}
}
@article{WollenbergerJinBernhardtetal.1998,
  author    = {Wollenberger, Ursula and Jin, Wen and Bernhardt, Rita and Lehmann, Claudia and St{\"o}cklein, Walter F. M. and Brigelius-Floh{\´e}, Regina and Scheller, Frieder W.},
  title     = {Funktionalisierung von Elektroden f{\"u}r den direkten heterogenen Elektrotransfer},
  year      = {1998},
  language  = {de}
}
@article{WollenbergerHintscheScheller1995,
  author    = {Wollenberger, Ursula and Hintsche, R. and Scheller, Frieder W.},
  title     = {Biosensors for analytical microsystems},
  year      = {1995},
  language  = {en}
}
@article{WollenbergerDrungilieneStoeckleinetal.1996,
  author    = {Wollenberger, Ursula and Drungiliene, A. and St{\"o}cklein, Walter F. M. and Kulys, J. and Scheller, Frieder W.},
  title     = {Direct electrocatalytic determination of dissolved peroxidases},
  year      = {1996},
  language  = {en}
}
@article{WollenbergerBistolasJungetal.2004,
  author    = {Wollenberger, Ursula and Bistolas, Nikitas and Jung, Christiane and Shumyantseva, V. V. and Ruzgas, T. and Scheller, Frieder W.},
  title     = {Elektroden-Design f{\"u}r elektronische Wechselwirkung mit Monooxygenasen},
  isbn      = {3-8047-2132-x},
  year      = {2004},
  language  = {de}
}
@phdthesis{Wollenberger2005,
  author    = {Wollenberger, Ursula},
  title     = {Kopplung von Biomolek{\"u}len mit Elektroden : von Bioelektrochemie zur Biosensorik},
  address   = {Potsdam},
  pages     = {Getr. Z{\"a}hlung : graph. Darst.},
  year      = {2005},
  language  = {de}
}
@article{Wollenberger1995,
  author    = {Wollenberger, Ursula},
  title     = {Electrochemical biosensors - ways to improve sensor performance},
  year      = {1995},
  language  = {en}
}
@article{Wollenberger2000,
  author    = {Wollenberger, Ursula},
  title     = {Integrierte Immuno-Extraktions-Probenahme und tragbarer Biosensor-Prototyp f{\"u}r vor-Ort Messungen},
  year      = {2000},
  language  = {de}
}
@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}
}