@article{JinWollenbergerScheller1998,
  author    = {Jin, Wen and Wollenberger, Ursula and Scheller, Frieder W.},
  title     = {PQQ as redox shuttle for quinoprotein glucose dehydrogenase},
  year      = {1998},
  language  = {en}
}
@article{LisdatHoWollenbergeretal.1998,
  author    = {Lisdat, Fred and Ho, Wah O. and Wollenberger, Ursula and Scheller, Frieder W. and Richter, Torsten and Bilitewski, Ursula},
  title     = {Recycling systems based on screen-printed electrodes},
  year      = {1998},
  language  = {en}
}
@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{LehmannWollenbergerBrigeliusFloheetal.1998,
  author    = {Lehmann, Claudia and Wollenberger, Ursula and Brigelius-Floh{\´e}, Regina and Scheller, Frieder W.},
  title     = {Bioelectrocatalysis by a selenoenzyme},
  year      = {1998},
  language  = {en}
}
@article{LisdatWollenbergerPaeschkeetal.1998,
  author    = {Lisdat, Fred and Wollenberger, Ursula and Paeschke, Manfred and Scheller, Frieder W.},
  title     = {Sensitive catecholamine measurement using a monoenzymatic recycling system},
  year      = {1998},
  language  = {en}
}
@article{KaatzStrefferWollenbergeretal.1999,
  author    = {Kaatz, Helvi and Streffer, Katrin and Wollenberger, Ursula and Peter, Martin G.},
  title     = {Inhibition of mushroom tyrosinase by kojic acid octanoates},
  year      = {1999},
  language  = {en}
}
@article{LeiLisdatWollenbergeretal.1999,
  author    = {Lei, Chenghong and Lisdat, Fred and Wollenberger, Ursula and Scheller, Frieder W.},
  title     = {Cytochrome c : Clay-modified electrode},
  year      = {1999},
  language  = {en}
}
@article{SchellerJinEhrentreichFoersteretal.1999,
  author    = {Scheller, Frieder W. and Jin, Wen and Ehrentreich-F{\"o}rster, Eva and Ge, Bixia and Lisdat, Fred and B{\"u}ttemeyer, R. and Wollenberger, Ursula},
  title     = {Cytochrome c based superoxide sensor for in vivo application},
  year      = {1999},
  language  = {en}
}
@article{GeMeyerSchoeningetal.2000,
  author    = {Ge, Bixia and Meyer, T. and Sch{\"o}ning, M. J. and Wollenberger, Ursula and Lisdat, Fred},
  title     = {Cytochrome c from chromatium vinosum on gold electrodes},
  year      = {2000},
  language  = {en}
}
@article{ChenWollenbergerLisdatetal.2000,
  author    = {Chen, Jian and Wollenberger, Ursula and Lisdat, Fred and Ge, Bixia and Scheller, Frieder W.},
  title     = {Superoxide sensor based on hemin modified electrode},
  year      = {2000},
  language  = {en}
}
@article{LeiWollenbergerJungetal.2000,
  author    = {Lei, Chenghong and Wollenberger, Ursula and Jung, Christiane and Scheller, Frieder W.},
  title     = {Clay-bridged electron transfer between cytochrome P450(cam) and electrode},
  year      = {2000},
  language  = {en}
}
@article{LeiWollenbergerScheller2000,
  author    = {Lei, Chenghong and Wollenberger, Ursula and Scheller, Frieder W.},
  title     = {Clay based direct electrochemistry of myoglobin},
  year      = {2000},
  language  = {en}
}
@article{FridmanWollenbergerBogdanovskayaetal.2000,
  author    = {Fridman, Vadim and Wollenberger, Ursula and Bogdanovskaya, V. A. and Lisdat, Fred and Ruzgas, T. and Lindgren, A. and Gorton, Lo and Scheller, Frieder W.},
  title     = {Electrochemical investigation of cellobiose oxidation by cellobiose dehydrogenase in the presence of cytochrome c as mediator},
  year      = {2000},
  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{WollenbergerJung2001,
  author    = {Wollenberger, Ursula and Jung, Christiane},
  title     = {Cytochrom P450-Elektrochemie},
  year      = {2001},
  language  = {de}
}
@article{LehmannWollenbergerBrigeliusFloheetal.2001,
  author    = {Lehmann, Claudia and Wollenberger, Ursula and Brigelius-Floh{\´e}, Regina and Scheller, Frieder W.},
  title     = {Modified gold electrodes for electrochemical studies of the reaction phospholipid hydroperoxide glutathione peroxidas with glutathione and glutathione disulfide},
  year      = {2001},
  language  = {en}
}
@article{SchellerBauerMarkoweretal.2001,
  author    = {Scheller, Frieder W. and Bauer, Christian G. and Markower, Alexander and Wollenberger, Ursula and Warsinke, Axel and Bier, Frank Fabian},
  title     = {Coupling of immunoassays with enzymatic recycling electrodes},
  year      = {2001},
  language  = {en}
}
@article{SchellerWollenbergerWarsinkeetal.2001,
  author    = {Scheller, Frieder W. and Wollenberger, Ursula and Warsinke, Axel and Lisdat, Fred},
  title     = {Research and development in biosensors},
  year      = {2001},
  language  = {en}
}
@article{RosePfeifferSchelleretal.2001,
  author    = {Rose, Andreas and Pfeiffer, Dorothea and Scheller, Frieder W. and Wollenberger, Ursula},
  title     = {Quinoprotein glucose dehydrogenasemodified thick-film electrodes for the amperometric detection of phenolic compounds in flow injection analysis},
  year      = {2001},
  language  = {en}
}
@article{VijgenboomVijgenboomTeppneretal.2001,
  author    = {Vijgenboom, E. and Vijgenboom, E. and Teppner, A. W. J. W. and Makower, Alexander and Scheller, Frieder W. and Canters, Gerard W. and Wollenberger, Ursula},
  title     = {Determination of phenolic compounds using recombinant tyrosinanse from Streptomyces antibioticus},
  year      = {2001},
  language  = {en}
}
@article{SchellerWollenbergerLeietal.2002,
  author    = {Scheller, Frieder W. and Wollenberger, Ursula and Lei, Chenghong and Jin, Wen and Ge, Bixia and Lehmann, Claudia and Lisdat, Fred and Fridman, Vadim},
  title     = {Bioelectrocatalysis by redox enzymes at modified electrodes},
  year      = {2002},
  language  = {en}
}
@article{NistorRoseFarreetal.2002,
  author    = {Nistor, C. and Rose, Andreas and Farre, M. and Stoica, L. and Wollenberger, Ursula and Ruzgas, T. and Pfeiffer, Dorothea and Barcelo, Damia and Gorton, Lo and Emneus, J.},
  title     = {In-field monitoring of cleaning efficiency in waste water treatment plants using two phenolsensitive biosensors},
  year      = {2002},
  language  = {en}
}
@article{LeiWollenbergerBistolasetal.2002,
  author    = {Lei, Chenghong and Wollenberger, Ursula and Bistolas, Nikitas and Guiseppi-Eli, A. and Scheller, Frieder W.},
  title     = {Electron transfer of hemoglobin at electrodes modified with colloidal clay nanoparticles},
  year      = {2002},
  language  = {en}
}
@article{NistorOsvikDavidssonetal.2002,
  author    = {Nistor, C. and Osvik, A. and Davidsson, R. and Rose, Andreas and Wollenberger, Ursula and Pfeiffer, Dorothea and Emneus, J. and Fiksdal, L.},
  title     = {Detection of escherichia coli water by culture-based amperometric and luminometric methods},
  year      = {2002},
  language  = {en}
}
@article{SchellerBauerMakoweretal.2002,
  author    = {Scheller, Frieder W. and Bauer, Christian G. and Makower, Alexander and Wollenberger, Ursula and Warsinke, Axel and Bier, Frank Fabian},
  title     = {Immunoassays using enzymatic amplification electrodes},
  isbn      = {0-7484-0791-X},
  year      = {2002},
  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{ChenStoeckleinSchelleretal.2003,
  author    = {Chen, Jian and St{\"o}cklein, Walter F. M. and Scheller, Frieder W. and Wollenberger, Ursula},
  title     = {Electrochemical determination of human hemoglobin by using ferrocene carboxylic acid modified carbon powder microelectrode},
  year      = {2003},
  language  = {en}
}
@article{SchellerWollenberger2003,
  author    = {Scheller, Frieder W. and Wollenberger, Ursula},
  title     = {Enzyme Electrodes},
  isbn      = {3-527-30401-0},
  year      = {2003},
  language  = {en}
}
@article{MakWollenbergerSchelleretal.2003,
  author    = {Mak, Karen K. W. and Wollenberger, Ursula and Scheller, Frieder W. and Renneberg, Reinhard},
  title     = {An amperometric bi-enzyme sensor for determination of formate using cofactor regeneration},
  year      = {2003},
  language  = {en}
}
@article{LoewSchellerWollenberger2004,
  author    = {Loew, Noya and Scheller, Frieder W. and Wollenberger, Ursula},
  title     = {Characterization of self-assembling of glucose dehydrogenase in mono- and multilayers on gold electrodes},
  year      = {2004},
  abstract  = {Glucose dehydrogenase (GDH) was assembled electrostatically onto QCM-gold electrodes by their sequential deposition with anionic polyelectrolytes such as PSS and PASA. For the layer-by-layer arrangements both the microgravimetric and the electrochemical sensor signal were followed. Increasing amounts of GDH were deposited by stepwise formation of alternating layers of GDH and PSS or PASA. The mass increase was about 1.88 mug/cm(2) for one GDH/ PASA bilayer and 2.4 mug/cm(2) for a GDH/PSS bilayer. The addition of phenolic compounds resulted in an oxidation current, which could be catalytically increased by the GDH catalysed reaction in the presence of glucose. The system functions as glucose sensor when quinones are present in nonlimiting amount. The amperometric response was already diffusion limited when a single layer of GDH was adsorbed. The sensor sensitivity increased by a factor of 10 when MSA was used instead of MUA as initial electrode modifier},
  language  = {en}
}
@article{KulysKrikstopaitisSchelleretal.2004,
  author    = {Kulys, J. and Krikstopaitis, K. and Scheller, Frieder W. and Wollenberger, Ursula},
  title     = {Electrochemical parameters of phenoxazine derivatives in solution and at monolayer-modified gold electrodes},
  year      = {2004},
  abstract  = {Electrochemical properties of beta-(10-phenoxazinyl) propylamine (APPX) and beta-(10-phenoxazinyl) propionic acid (PPX) have been studied in solution, and in immobilized state on gold electrodes modified with monolayers of cystamine and mercaptoundecanoic acid. A reversible diffusion-controlled process of APPX and PPX was observed at a bare gold electrode. The electrochemical conversion of both compounds at modified gold electrodes was a quasireversible diffusion-controlled process. The redox potential of immobilized APPX (443 mV) was similar to the potential in solution, while the value of the immobilized PPX was 131 mV higher than in solution. The immobilized mediators were electrocatalytically active in the fungal peroxidase-catalyzed hydrogen peroxide reduction},
  language  = {en}
}
@article{BistolasChristensonRuzgasetal.2004,
  author    = {Bistolas, Nikitas and Christenson, A. and Ruzgas, T. and Jung, Christiane and Scheller, Frieder W. and Wollenberger, Ursula},
  title     = {Spectroelectrochemistry of cytochrome P450cam},
  year      = {2004},
  abstract  = {The spectroelectrochemistry of camphor-bound cytochrome P450cam (P450cam) using gold electrodes is described. The electrodes were modified with either 4,4'-dithiodipyridin or sodium dithionite. Electrolysis of P450cam was carried out when the enzyme was in solution, while at the same time UV visible absorption spectra were recorded. Reversible oxidation and reduction could be observed with both 4,4'-dithiodipyridin and dithionite modified electrodes. A formal potential (E-0') of -373 mV vs Ag/AgCl 1 M KCl was determined. The spectra of P450cam complexed with either carbon monoxide or metyrapone, both being inhibitors of P450 catalysis, clearly indicated that the protein retained its native state in the electrochemical cell during electrolysis. (C) 2003 Elsevier Inc. All rights reserved},
  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}
}
@article{KroeningSchellerWollenbergeretal.2004,
  author    = {Kr{\"o}ning, Steffen and Scheller, Frieder W. and Wollenberger, Ursula and Lisdat, Fred},
  title     = {Myoglobin-Clay Electrode for Nitric Oxide (NO) Detection in Solution},
  year      = {2004},
  language  = {en}
}
@article{LiuWollenbergerHalameketal.2005,
  author    = {Liu, Songqin and Wollenberger, Ursula and Halamek, Jan and Leupold, Eik and St{\"o}cklein, Walter F. M. and Warsinke, Axel and Scheller, Frieder W.},
  title     = {Affinity interaction betwen phenylboronic acid-carrying self-assembled monolayers and FAD or HRP},
  year      = {2005},
  abstract  = {A method is provided for the recognition of glycated molecules based on their binding affinities to boronate- carrying monolayers. The affinity interaction of flavin adenine dinucleotide (FAD) and horseradish peroxidase (HRP) with phenylboronic acid monolayers on gold was investigated by using voltammetric and microgravimetric methods. Conjugates of 3-aminopherrylboronic acid and 3,3'-dithiodipropionic acid di(N-hydroxysuccinimide ester) or 11-mercaptoundecanoic acid were prepared and self-assembled on gold surfaces to generate monolayers. FAD is bound to this modified sur-face and recognized by a pair of redox peaks with a formal potential of -0.433 V in a 0.1 m phosphate buffer solution, pH 6.5. Upon addition of a sugar to the buffer, the bound FAD could be replaced, indicating that the binding is reversible. Voltammetric, mass measurements, and photometric activity assays show that the HRP can also be bound to the interface. This binding is reversible, and HRP can be replaced by sorbitol or removed in acidic solution. The effects of pH, incubation time, and concentration of H2O2 were studied by comparing the catalytic reduction of H2O2 in the presence of the electron-donor thionine. The catalytic current of the HRP-loaded electrode was proportional to HRP concentrations in the incubation solution in the range between 5 mu g mL(-1) and 0.4 mg mL(-1) with a linear slope of 3.34 mu A mL mg(-1) and a correlation coefficient of 0.9945},
  language  = {en}
}
@article{BistolasWollenbergerJungetal.2005,
  author    = {Bistolas, Nikitas and Wollenberger, Ursula and Jung, Christiane and Scheller, Frieder W.},
  title     = {Cytochrome P450 biosensors : a review},
  year      = {2005},
  abstract  = {Cytochrome P450 (CYP) is a large family of enzymes containing heme as the active site. Since their discovery and the elucidation of their structure, they have attracted the interest of scientist for many years, particularly due to their catalytic abilities. Since the late 1970s attempts have concentrated on the construction and development of electrochemical sensors. Although sensors based on mediated electron transfer have also been constructed, the direct electron transfer approach has attracted most of the interest. This has enabled the investigation of the electrochemical properties of the various isoforms of CYP. Furthermore, CYP utilized to construct biosensors for the determination of substrates important in environmental monitoring, pharmaceutical industry and clinical practice. (c) 2004 Elsevier B. V. All rights reserved},
  language  = {en}
}
@article{SchellerBistolasLiuetal.2005,
  author    = {Scheller, Frieder W. and Bistolas, Nikitas and Liu, Songqin and J{\"a}nchen, Michael and Katterle, Martin and Wollenberger, Ursula},
  title     = {Thirty years of haemoglobin electrochemistry},
  year      = {2005},
  abstract  = {Electrochemical investigations of the blood oxygen carrier protein include both mediated and direct electron transfer. The reaction of haemoglobin (Hb) with typical mediators, e.g., ferricyanide, can be quantified by measuring the produced ferrocyanide which is equivalent to the Hb concentration. Immobilization of the mediator within the electrode body allows reagentless electrochemical measuring of Hb. On the other hand, entrapment of the protein within layers of polyclectrolytes, lipids, nanoparticles of clay or gold leads to a fast heterogeneous electron exchange of the partially denatured Hb. (c) 2005 Elsevier B.V. All rights reserved},
  language  = {en}
}
@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{SchellerLisdatWollenberger2005,
  author    = {Scheller, Frieder W. and Lisdat, Fred and Wollenberger, Ursula},
  title     = {Application of electrically contacted enzymes for biosensors},
  isbn      = {3-527- 30690-0},
  year      = {2005},
  language  = {en}
}
@article{SezerSpricigoUteschetal.2010,
  author    = {Sezer, Murat and Spricigo, Roberto and Utesch, Tillmann and Millo, Diego and Leimk{\"u}hler, Silke and Mroginski, Maria A. and Wollenberger, Ursula and Hildebrandt, Peter and Weidinger, Inez M.},
  title     = {Redox properties and catalytic activity of surface-bound human sulfite oxidase studied by a combined surface enhanced resonance Raman spectroscopic and electrochemical approach},
  issn      = {1463-9076},
  doi       = {10.1039/B927226g},
  year      = {2010},
  abstract  = {Human sulfite oxidase (hSO) was immobilised on SAM-coated silver electrodes under preservation of the native heme pocket structure of the cytochrome b5 (Cyt b5) domain and the functionality of the enzyme. The redox properties and catalytic activity of the entire enzyme were studied by surface enhanced resonance Raman (SERR) spectroscopy and cyclic voltammetry (CV) and compared to the isolated heme domain when possible. It is shown that heterogeneous electron transfer and catalytic activity of hSO sensitively depend on the local environment of the enzyme. Increasing the ionic strength of the buffer solution leads to an increase of the heterogeneous electron transfer rate from 17 s(-1) to 440 s(- 1) for hSO as determined by SERR spectroscopy. CV measurements demonstrate an increase of the apparent turnover rate for the immobilised hSO from 0.85 s(-1) in 100 mM buffer to 5.26 s(-1) in 750 mM buffer. We suggest that both effects originate from the increased mobility of the surface-bound enzyme with increasing ionic strength. In agreement with surface potential calculations we propose that at high ionic strength the enzyme is immobilised via the dimerisation domain to the SAM surface. The flexible loop region connecting the Moco and the Cyt b5 domain allows alternating contact with the Moco interaction site and the SAM surface, thereby promoting the sequential intramolecular and heterogeneous electron transfer from Moco via Cyt b5 to the electrode. At lower ionic strength, the contact time of the Cyt b5 domain with the SAM surface is longer, corresponding to a slower overall electron transfer process.},
  language  = {en}
}
@article{LiuWollenbergerKatterleetal.2006,
  author    = {Liu, Songqin and Wollenberger, Ursula and Katterle, Martin and Scheller, Frieder W.},
  title     = {Ferroceneboronic acid-based amperometric biosensor for glycated hemoglobin},
  issn      = {0925-4005},
  doi       = {10.1016/j.snb.2005.07.011},
  year      = {2006},
  abstract  = {An amperometric biosensor for the determination of glycated hemoglobin in human whole blood is proposed. The principle is based on the electrochemical measurement of ferroceneboronic acid (FcBA) that has been specifically bound to the glycated N-terminus. Hemoglobin is immobilized on a zirconium dioxide nanoparticle modified pyrolytic graphite electrode (PGE) in the presence of didodecyldimethylammonium bromide (DDAB). The incubation of this sensor in FcBA solution leads to the formation of an FcBA-modified surface due to the affinity interaction between boronate and the glycated sites of the hemoglobin. The binding of FcBA results in well-defined redox peaks with an E-0' of 0.299 V versus Ag/AgCl (1 M KCl). The square wave voltammetric response of the bound FcBA reflects the amount of glycated hemoglobin at the surface. This signal increases linearily with the degree of glycated hemoglobin from 6.8 to 14.0\% of total immobilized hemoglobin. The scheme was applied to the determination of the fraction of glycated hemoglobin in whole blood samples.},
  language  = {en}
}
@misc{ZorHeiskanenCavigliaetal.2014,
  author    = {Z{\´o}r, K. and Heiskanen, A. and Caviglia, Claudia and Vergani, M. and Landini, E. and Shah, F. and Carminati, Marco and Mart{\´i}nez-Serrano, A. and Ramos Moreno, T. and Kokaia, M. and Benayahu, Dafna and Keresztes, Zs. and Papkovsky, D. and Wollenberger, Ursula and Svendsen, W. E. and Dimaki, M. and Ferrari, G. and Raiteri, R. and Sampietro, M. and Dufva, M. and Emn{\´e}us, J.},
  title     = {A compact multifunctional microfluidic platform for exploring cellular dynamics in real-time using electrochemical detection},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-99492},
  pages     = {11},
  year      = {2014},
  abstract  = {Downscaling of microfluidic cell culture and detection devices for electrochemical monitoring has mostly focused on miniaturization of the microfluidic chips which are often designed for specific applications and therefore lack functional flexibility. We present a compact microfluidic cell culture and electrochemical analysis platform with in-built fluid handling and detection, enabling complete cell based assays comprising on-line electrode cleaning, sterilization, surface functionalization, cell seeding, cultivation and electrochemical real-time monitoring of cellular dynamics. To demonstrate the versatility and multifunctionality of the platform, we explored amperometric monitoring of intracellular redox activity in yeast (Saccharomyces cerevisiae) and detection of exocytotically released dopamine from rat pheochromocytoma cells (PC12). Electrochemical impedance spectroscopy was used in both applications for monitoring cell sedimentation and adhesion as well as proliferation in the case of PC12 cells. The influence of flow rate on the signal amplitude in the detection of redox metabolism as well as the effect of mechanical stimulation on dopamine release were demonstrated using the programmable fluid handling capability. The here presented platform is aimed at applications utilizing cell based assays, ranging from e.g. monitoring of drug effects in pharmacological studies, characterization of neural stem cell differentiation, and screening of genetically modified microorganisms to environmental monitoring.},
  language  = {en}
}