@article{BauerEremenkoEhrentreichFoersteretal.1996,
  author    = {Bauer, Christian G. and Eremenko, A. V. and Ehrentreich-F{\"o}rster, Eva and Bier, Frank Fabian and Makower, Alexander and Halsall, H. B. and Heineman, W. R. and Scheller, Frieder W.},
  title     = {Zeptomole-detecting biosensor for alkaline phosphatase in an electroche mical immunoassay for 2,4- dichlorophenoacetic acid},
  year      = {1996},
  language  = {en}
}
@article{SchellerSchubertBier1995,
  author    = {Scheller, Frieder W. and Schubert, Florian and Bier, Frank Fabian},
  title     = {Vom Biosensor zur Nanobiotechnologie},
  year      = {1995},
  language  = {de}
}
@article{JetzschmannJagerszkiDechtriratetal.2015,
  author    = {Jetzschmann, Katharina J. and Jagerszki, Gyula and Dechtrirat, Decha and Yarman, Aysu and Gajovic-Eichelmann, Nenad and Gilsing, Hans-Detlev and Schulz, Burkhard and Gyurcsanyi, Robert E. and Scheller, Frieder W.},
  title     = {Vectorially Imprinted Hybrid Nanofilm for Acetylcholinesterase Recognition},
  series = {Advanced functional materials},
  volume    = {25},
  journal   = {Advanced functional materials},
  number    = {32},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1616-301X},
  doi       = {10.1002/adfm.201501900},
  pages     = {5178 -- 5183},
  year      = {2015},
  abstract  = {Effective recognition of enzymatically active tetrameric acetylcholinesterase (AChE) is accomplished by a hybrid nanofilm composed of a propidium-terminated self-assembled monolayer (Prop-SAM) which binds AChE via its peripheral anionic site (PAS) and an ultrathin electrosynthesized molecularly imprinted polymer (MIP) cover layer of a novel carboxylate-modified derivative of 3,4-propylenedioxythiophene. The rebinding of the AChE to the MIP/Prop-SAM nanofilm covered electrode is detected by measuring in situ the enzymatic activity. The oxidative current of the released thiocholine is dependent on the AChE concentration from approximate to 0.04 x 10(-6) to 0.4 x 10(-6)m. An imprinting factor of 9.9 is obtained for the hybrid MIP, which is among the best values reported for protein imprinting. The dissociation constant characterizing the strength of the MIP-AChE binding is 4.2 x 10(-7)m indicating the dominant role of the PAS-Prop-SAM interaction, while the benefit of the MIP nanofilm covering the Prop-SAM layer is the effective suppression of the cross-reactivity toward competing proteins as compared with the Prop-SAM. The threefold selectivity gain provided by i) the shape-specific MIP filter, ii) the propidium-SAM, iii) signal generation only by the AChE bound to the nanofilm shows promise for assessing AChE activity levels in cerebrospinal fluid.},
  language  = {en}
}
@incollection{AscheBoeckmannLaueetal.2000,
  author    = {Asche, Hartmut and B{\"o}ckmann, Christine and Laue, Steffen and L{\"o}hmannsr{\"o}ben, Hans-Gerd and Lemke, Matthias and Schober, Lars and Reich, Oliver and L{\"u}ck, Erika and Sch{\"u}tte, Marc and Domsch, Horst and Makower, Alexander and Scheller, Frieder W. and St{\"o}cklein, Wolfgang and Wollenberger, Ursula and Schultze, Rainer and Hengstermann, Theo and Schael, Frank},
  title     = {Umweltforschung f{\"u}r das Land Brandenburg : Projekt Umweltanalytik / Umweltmeßtechnik / Informationssysteme},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus-3862},
  publisher      = {Universit{\"a}t Potsdam},
  pages     = {176 -- 227},
  year      = {2000},
  language  = {de}
}
@incollection{LueckBalderjahnKammetal.2000,
  author    = {L{\"u}ck, Erika and Balderjahn, Ingo and Kamm, Birgit and Greil, Holle and Wallschl{\"a}ger, Hans-Dieter and Jessel, Beate and B{\"o}ckmann, Christine and Oberh{\"a}nsli, Roland and Soyez, Konrad and Schmeer, Ernst and Blumenstein, Oswald and Berndt, Klaus-Peter and Edeling, Thomas and Friedrich, Sabine and Kaden, Klaus and Scheller, Frieder W. and Petersen, Hans-Georg and Asche, Hartmut and Bronstert, Axel and Giest, Hartmut and Gaedke, Ursula and L{\"o}hmannsr{\"o}ben, Hans-Gerd and Jeltsch, Florian and J{\"a}nkel, Ralph and Gzik, Axel and Bork, Hans-Rudolf and Bork, Hans-Rudolf},
  title     = {Umweltforschung f{\"u}r das Land Brandenburg : Arbeitsgruppen und Professuren},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus-3797},
  publisher      = {Universit{\"a}t Potsdam},
  year      = {2000},
  language  = {de}
}
@article{BierEhrentreichFoersterSchelleretal.1996,
  author    = {Bier, Frank Fabian and Ehrentreich-F{\"o}rster, Eva and Scheller, Frieder W. and Makower, Alexander and Eremenko, A. V. and Wollenberger, Ursula and Bauer, Christian G. and Pfeiffer, Dorothea and Micheel, Burkhard},
  title     = {Ultrasensitive biosensors},
  year      = {1996},
  language  = {en}
}
@article{SzeponikMoellerPfeifferetal.1997,
  author    = {Szeponik, Jan and M{\"o}ller, B. and Pfeiffer, Dorothea and Lisdat, Fred and Wollenberger, Ursula and Makower, Alexander and Scheller, Frieder W.},
  title     = {Ultrasensitive bienzyme sensor for adrenaline},
  year      = {1997},
  language  = {en}
}
@article{MakowerEremenkoStrefferetal.1996,
  author    = {Makower, Alexander and Eremenko, A. V. and Streffer, Katrin and Wollenberger, Ursula and Scheller, Frieder W.},
  title     = {Tyrosinase-glucose dehydrogenase substrate-recycling biosensor : a highly sensitive measurement of phenolic compounds},
  year      = {1996},
  language  = {en}
}
@article{Scheller2009,
  author    = {Scheller, Frieder W.},
  title     = {Tribute to Guenter Gauglitz (Editorial)},
  issn      = {1618-2642},
  doi       = {10.1007/s00216-008-2548-0},
  year      = {2009},
  language  = {en}
}
@article{SchellerBier2002,
  author    = {Scheller, Frieder W. and Bier, Frank Fabian},
  title     = {Trends in der Bioanalytik},
  year      = {2002},
  language  = {de}
}
@article{NiessnerBroekaertEinaxetal.2002,
  author    = {Nießner, Reinhard and Broekaert, J. and Einax, J. W. and Scheller, Frieder W. and St{\"o}cklein, Walter F. M.},
  title     = {Trendbericht analytische Biochemie 2000/2001},
  year      = {2002},
  language  = {de}
}
@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}
}
@article{YarmanSchulzSygmundetal.2014,
  author    = {Yarman, Aysu and Schulz, Christopher and Sygmund, Cristoph and Ludwig, Roland and Gorton, Lo and Wollenberger, Ursula and Scheller, Frieder W.},
  title     = {Third generation ATP sensor with enzymatic analyte recycling},
  series = {Electroanalysis : an international journal devoted to fundamental and practical aspects of electroanalysis},
  volume    = {26},
  journal   = {Electroanalysis : an international journal devoted to fundamental and practical aspects of electroanalysis},
  number    = {9},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1040-0397},
  doi       = {10.1002/elan.201400231},
  pages     = {2043 -- 2048},
  year      = {2014},
  abstract  = {For the first time the direct electron transfer of an enzyme - cellobiose dehydrogenase, CDH - has been coupled with the hexokinase catalyzed competition for glucose in a sensor for ATP. To enhance the signal output for ATP, pyruvate kinase was coimmobilized to recycle ADP by the phosphoenolpyruvate driven reaction. The new sensor overcomes the limit of 1:1 stoichiometry of the sequential or competitive conversion of ATP by effective enzymatic recycling of the analyte. The anodic oxidation of the glucose converting CDH proceeds at electrode potentials below 0 mV vs. Ag vertical bar AgCl thus potentially interfering substances like ascorbic acid or catecholamines do not influence the measuring signal. The combination of direct electron transfer of CDH with the enzymatic recycling results in an interference-free and oxygen-independent measurement of ATP in the lower mu molar concentration range with a lower limit of detection of 63.3 nM (S/N=3).},
  language  = {en}
}
@article{KrylovBeissenhirtzAdamzigetal.2004,
  author    = {Krylov, Andrey V. and Beissenhirtz, Moritz Karl and Adamzig, Holger and Scheller, Frieder W. and Lisdat, Fred},
  title     = {Thick-film electrodes for measurement of superoxide and hydrogen peroxide based on direct protein-electrode contacts},
  year      = {2004},
  abstract  = {Cytochrome c was immobilized on screen-printed thick-film gold electrodes by a self-assembly approach using mixed monolayers of mercaptoundecanoic acid and mercaptoundecanol. Cyclic voltammetry revealed quasi-reversible electrochemical behavior of the covalently fixed protein with a formal potential of +10 mV vs. Ag/AgCl. Polarized at +150 mV vs. Ag/AgCl the electrode was found to be sensitive to superoxide radicals in the range 300-1200 nmol L-1. Compared with metal needle electrodes sensitivity and reproducibility could be improved and combined with the easiness of preparation. This allows the fabrication of disposable sensors for nanomolar superoxide concentrations. By changing the electrode potential the sensor can be switched from response to superoxide radicals to hydrogen peroxide-another reactive oxygen species. H2O2 sensitivity can be provided in the range 10-1000 mumol L-1 which makes the electrode suitable for oxidative stress studies},
  language  = {en}
}
@article{SchulmeisterScheller1996,
  author    = {Schulmeister, Thomas and Scheller, Frieder W.},
  title     = {The mathematics of exponential signal amplification in amperometric three enzyme electrodes},
  year      = {1996},
  language  = {en}
}
@article{YarmanScheller2014,
  author    = {Yarman, Aysu and Scheller, Frieder W.},
  title     = {The first electrochemical MIP sensor for tamoxifen},
  series = {Sensors},
  volume    = {14},
  journal   = {Sensors},
  number    = {5},
  publisher = {MDPI},
  address   = {Basel},
  issn      = {1424-8220},
  doi       = {10.3390/s140507647},
  pages     = {7647 -- 7654},
  year      = {2014},
  abstract  = {We present an electrochemical MIP sensor for tamoxifen (TAM)-a nonsteroidal anti-estrogen-which is based on the electropolymerisation of an O-phenylenediamine. resorcinol mixture directly on the electrode surface in the presence of the template molecule. Up to now only. bulk. MIPs for TAM have been described in literature, which are applied for separation in chromatography columns. Electro-polymerisation of the monomers in the presence of TAM generated a film which completely suppressed the reduction of ferricyanide. Removal of the template gave a markedly increased ferricyanide signal, which was again suppressed after rebinding as expected for filling of the cavities by target binding. The decrease of the ferricyanide peak of the MIP electrode depended linearly on the TAM concentration between 1 and 100 nM. The TAM-imprinted electrode showed a 2.3 times higher recognition of the template molecule itself as compared to its metabolite 4-hydroxytamoxifen and no cross-reactivity with the anticancer drug doxorubucin was found. Measurements at + 1.1 V caused a fouling of the electrode surface, whilst pretreatment of TAM with peroxide in presence of HRP generated an oxidation product which was reducible at 0 mV, thus circumventing the polymer formation and electrochemical interferences.},
  language  = {en}
}
@misc{YarmanScheller2014,
  author    = {Yarman, Aysu and Scheller, Frieder W.},
  title     = {The first electrochemical MIP sensor for tamoxifen},
  series = {Postprints der Universit{\"a}t Potsdam : Mathematisch-Naturwissenschaftliche Reihe},
  journal   = {Postprints der Universit{\"a}t Potsdam : Mathematisch-Naturwissenschaftliche Reihe},
  number    = {1046},
  issn      = {1866-8372},
  doi       = {10.25932/publishup-47617},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-476173},
  pages     = {10},
  year      = {2014},
  abstract  = {We present an electrochemical MIP sensor for tamoxifen (TAM)-a nonsteroidal anti-estrogen-which is based on the electropolymerisation of an O-phenylenediamine. resorcinol mixture directly on the electrode surface in the presence of the template molecule. Up to now only. bulk. MIPs for TAM have been described in literature, which are applied for separation in chromatography columns. Electro-polymerisation of the monomers in the presence of TAM generated a film which completely suppressed the reduction of ferricyanide. Removal of the template gave a markedly increased ferricyanide signal, which was again suppressed after rebinding as expected for filling of the cavities by target binding. The decrease of the ferricyanide peak of the MIP electrode depended linearly on the TAM concentration between 1 and 100 nM. The TAM-imprinted electrode showed a 2.3 times higher recognition of the template molecule itself as compared to its metabolite 4-hydroxytamoxifen and no cross-reactivity with the anticancer drug doxorubucin was found. Measurements at + 1.1 V caused a fouling of the electrode surface, whilst pretreatment of TAM with peroxide in presence of HRP generated an oxidation product which was reducible at 0 mV, thus circumventing the polymer formation and electrochemical interferences.},
  language  = {en}
}
@article{SpricigoLeimkuehlerGortonetal.2015,
  author    = {Spricigo, Roberto and Leimk{\"u}hler, Silke and Gorton, Lo and Scheller, Frieder W. and Wollenberger, Ursula},
  title     = {The Electrically Wired Molybdenum Domain of Human Sulfite Oxidase is Bioelectrocatalytically Active},
  series = {European journal of inorganic chemistry : a journal of ChemPubSoc Europe},
  journal   = {European journal of inorganic chemistry : a journal of ChemPubSoc Europe},
  number    = {21},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1434-1948},
  doi       = {10.1002/ejic.201500034},
  pages     = {3526 -- 3531},
  year      = {2015},
  abstract  = {We report electron transfer between the catalytic molybdenum cofactor (Moco) domain of human sulfite oxidase (hSO) and electrodes through a poly(vinylpyridine)-bound [osmium(N,N'-methyl-2,2'-biimidazole)(3)](2+/3+) complex as the electron-transfer mediator. The biocatalyst was immobilized in this low-potential redox polymer on a carbon electrode. Upon the addition of sulfite to the immobilized separate Moco domain, the generation of a significant catalytic current demonstrated that the catalytic center is effectively wired and active. The bioelectrocatalytic current of the wired separate catalytic domain reached 25\% of the signal of the wired full molybdoheme enzyme hSO, in which the heme b(5) is involved in the electron-transfer pathway. This is the first report on a catalytically active wired molybdenum cofactor domain. The formal potential of this electrochemical mediator is between the potentials of the two cofactors of hSO, and as hSO can occupy several conformations in the polymer matrix, it is imaginable that electron transfer from the catalytic site to the electrode through the osmium center occurs for the hSO molecules in which the Moco domain is sufficiently accessible. The observation of catalytic oxidation currents at low potentials is favorable for applications in bioelectronic devices.},
  language  = {en}
}
@article{EremenkoBauerMakoweretal.1998,
  author    = {Eremenko, Arkadi V. and Bauer, Christian G. and Makower, Alexander and Kanne, Beate and Baumgarten, Horst and Scheller, Frieder W.},
  title     = {The development of a non-competitive immunoenzymometric Assay (IEMA) of cocaine},
  year      = {1998},
  language  = {en}
}
@article{HuangWarsinkeKuwanaetal.1998,
  author    = {Huang, T. and Warsinke, Axel and Kuwana, T. and Scheller, Frieder W.},
  title     = {The determination of L-phenylalanine based on a novel NADH-detecting biosensor},
  year      = {1998},
  language  = {en}
}
@article{YarmanGroebeNeumannetal.2012,
  author    = {Yarman, Aysu and Gr{\"o}be, Glenn and Neumann, Bettina and Kinne, Mathias and Gajovic-Eichelmann, Nenad and Wollenberger, Ursula and Hofrichter, Martin and Ullrich, Rene and Scheibner, Katrin and Scheller, Frieder W.},
  title     = {The aromatic peroxygenase from Marasmius rutola-a new enzyme for biosensor applications},
  series = {Analytical \& bioanalytical chemistry},
  volume    = {402},
  journal   = {Analytical \& bioanalytical chemistry},
  number    = {1},
  publisher = {Springer},
  address   = {Heidelberg},
  issn      = {1618-2642},
  doi       = {10.1007/s00216-011-5497-y},
  pages     = {405 -- 412},
  year      = {2012},
  abstract  = {The aromatic peroxygenase (APO; EC 1.11.2.1) from the agraric basidomycete Marasmius rotula (MroAPO) immobilized at the chitosan-capped gold-nanoparticle-modified glassy carbon electrode displayed a pair of redox peaks with a midpoint potential of -278.5 mV vs. AgCl/AgCl (1 M KCl) for the Fe(2+)/Fe(3+) redox couple of the heme-thiolate-containing protein. MroAPO oxidizes aromatic substrates such as aniline, p-aminophenol, hydroquinone, resorcinol, catechol, and paracetamol by means of hydrogen peroxide. The substrate spectrum overlaps with those of cytochrome P450s and plant peroxidases which are relevant in environmental analysis and drug monitoring. In M. rotula peroxygenase-based enzyme electrodes, the signal is generated by the reduction of electrode-active reaction products (e.g., p-benzoquinone and p-quinoneimine) with electro-enzymatic recycling of the analyte. In these enzyme electrodes, the signal reflects the conversion of all substrates thus representing an overall parameter in complex media. The performance of these sensors and their further development are discussed.},
  language  = {en}
}
@article{LisdatScheller2000,
  author    = {Lisdat, Fred and Scheller, Frieder W.},
  title     = {Technical principles. Electrodes},
  isbn      = {90-5702-447-7},
  year      = {2000},
  language  = {en}
}
@article{PengUteschYarmanetal.2015,
  author    = {Peng, Lei and Utesch, Tillmann and Yarman, Aysu and Jeoung, Jae-Hun and Steinborn, Silke and Dobbek, Holger and Mroginski, Maria Andrea and Tanne, Johannes and Wollenberger, Ursula and Scheller, Frieder W.},
  title     = {Surface-Tuned Electron Transfer and Electrocatalysis of Hexameric Tyrosine-Coordinated Heme Protein},
  series = {Chemistry - a European journal},
  volume    = {21},
  journal   = {Chemistry - a European journal},
  number    = {20},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {0947-6539},
  doi       = {10.1002/chem.201405932},
  pages     = {7596 -- 7602},
  year      = {2015},
  abstract  = {Molecular modeling, electrochemical methods, and quartz crystal microbalance were used to characterize immobilized hexameric tyrosine-coordinated heme protein (HTHP) on bare carbon or on gold electrodes modified with positively and negatively charged self-assembled monolayers (SAMs), respectively. HTHP binds to the positively charged surface but no direct electron transfer (DET) is found due to the long distance of the active sites from the electrode surfaces. At carboxyl-terminated surfaces, the neutrally charged bottom of HTHP can bind to the SAM. For this "disc" orientation all six hemes are close to the electrode and their direct electron transfer should be efficient. HTHP on all negatively charged SAMs showed a quasi-reversible redox behavior with rate constant k(s) values between 0.93 and 2.86 s(-1) and apparent formal potentials E-app(0)' between -131.1 and -249.1 mV. On the MUA/MU-modified electrode, the maximum surface concentration corresponds to a complete monolayer of the hexameric HTHP in the disc orientation. HTHP electrostatically immobilized on negatively charged SAMs shows electrocatalysis of peroxide reduction and enzymatic oxidation of NADH.},
  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{SpricigoRichterLeimkuehleretal.2010,
  author    = {Spricigo, Roberto and Richter, Claudia and Leimk{\"u}hler, Silke and Gorton, Lo and Scheller, Frieder W. and Wollenberger, Ursula},
  title     = {Sulfite biosensor based on osmium redox polymer wired sulfite oxidase},
  issn      = {0927-7757},
  doi       = {10.1016/j.colsurfa.2009.09.001},
  year      = {2010},
  abstract  = {A biosensor, based on a redoxactive osmium polymer and sulfite oxidase on screen-printed electrodes, is presented here as a promising method for the detection of sulfite. A catalytic oxidative current was generated when a sample containing sulfite was pumped over the carbon screen-printed electrode modified with osmium redox polymer wired sulfite oxidase. A stationary value was reached after approximately 50 s and a complete measurement lasted no more than 3 min. The electrode polarized at -0.1 V (vs. Ag vertical bar AgCl 1M KCl) permits minimizing the influence of interfering substances, since these compounds can be unspecific oxidized at higher potentials. Because of the good stability of the protein film on the electrode surface, a well functioning biosensor-flow system was possible to construct. The working stability and reproducibility were further enhanced by the addition of bovine serum albumin generating a more long-term stable and biocompatible protein environment. The optimized biosensor showed a stable signal for more than a week of operation and a coefficient of variation of 4.8\% for 12 successive measurements. The lower limit of detection of the sensor was 0.5 mu M sulfite and the response was linear until 100 mu M. The high sensitivity permitted a 1:500 dilution of wine samples. The immobilization procedure and the operational conditions granted minimized interferences. Additionally, repeating the immobilization procedure to form several layers of wired SO further increased the sensitivity of such a sensor. Finally. the applicability of the developed sulfite biosensor was tested on real samples, such as white and red wines.},
  language  = {en}
}
@article{EhrentreichFoersterShishniashviliSongetal.1998,
  author    = {Ehrentreich-F{\"o}rster, Eva and Shishniashvili, D. and Song, Min Ik and Scheller, Frieder W.},
  title     = {Study of antioxidative substances by means of a ssuperoxide sensor},
  year      = {1998},
  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{LisdatGeEhrentreichFoersteretal.1999,
  author    = {Lisdat, Fred and Ge, Bixia and Ehrentreich-F{\"o}rster, Eva and Reszka, R. and Scheller, Frieder W.},
  title     = {SOD activity measurement using cytochrome c modified electrode},
  year      = {1999},
  language  = {en}
}
@phdthesis{BenkertSchellerSchoessleretal.2000,
  author    = {Benkert, Alexander and Scheller, Frieder W. and Sch{\"o}ssler, W. and Micheel, Burkhard and Warsinke, Axel},
  title     = {Size exclusion redox-labeled immunoassay (SERI) : a new format for homogeneous amperometric creatinine determination},
  year      = {2000},
  language  = {en}
}
@article{YarmanKurbanoğluZebgeretal.2021,
  author    = {Yarman, Aysu and Kurbanoğlu, Sevin{\c{c}} and Zebger, Ingo and Scheller, Frieder W.},
  title     = {Simple and robust},
  series = {Sensors and actuators : B, Chemical : an international journal devoted to research and development of chemical transducers},
  volume    = {330},
  journal   = {Sensors and actuators : B, Chemical : an international journal devoted to research and development of chemical transducers},
  publisher = {Elsevier Science},
  address   = {Amsterdam [u.a.]},
  issn      = {0925-4005},
  doi       = {10.1016/j.snb.2020.129369},
  pages     = {12},
  year      = {2021},
  abstract  = {A spectrum of 7562 publications on Molecularly Imprinted Polymers (MIPs) has been presented in literature within the last ten years (Scopus, September 7, 2020). Around 10 \% of the papers published on MIPs describe the recognition of proteins. The straightforward synthesis of MIPs is a significant advantage as compared with the preparation of enzymes or antibodies. MIPs have been synthesized from only one up to six functional monomers while proteins are made up of 20 natural amino acids. Furthermore, they can be synthesized against structures of low immunogenicity and allow multi-analyte measurements via multi-target synthesis. Electrochemical methods allow simple polymer synthesis, removal of the template and readout. Among the different sensor configurations electrochemical MIP-sensors provide the broadest spectrum of protein analytes. The sensitivity of MIP-sensors is sufficiently high for biomarkers in the sub-nanomolar region, nevertheless the cross-reactivity of highly abundant proteins in human serum is still a challenge. MIPs for proteins offer innovative tools not only for clinical and environmental analysis, but also for bioimaging, therapy and protein engineering.},
  language  = {en}
}
@article{LisdatGeMeyerhoffetal.2001,
  author    = {Lisdat, Fred and Ge, Bixia and Meyerhoff, M. E. and Scheller, Frieder W.},
  title     = {Signal chains with cytochromes at SAM modified gold electrodes},
  year      = {2001},
  language  = {en}
}
@article{HalamekWollenbergerStoeckleinetal.2007,
  author    = {Hal{\´a}mek, Jan and Wollenberger, Ursula and St{\"o}cklein, Walter F. M. and Warsinke, Axel and Scheller, Frieder W.},
  title     = {Signal amplification in immunoassays using labeling via boronic acid binding to the sugar moiety of immunoglobulin G : proof of concept for glycated hemoglobin},
  issn      = {0003-2719},
  doi       = {10.1080/00032710701327096},
  year      = {2007},
  abstract  = {A novel electrochemical immunoassay based on the multiple affinity labeling of the indicator antibody with an electro-active tag is presented. The concept is illustrated for the determination of the glycated hemoglobin HbA1c in hemoglobin samples. Hemoglobin is adsorbed to the surfactant-modified surface of a piezoelectric quartz crystal. Whereas the quartz crystal nanobalance is used to validate the total Hb binding, the HbA1c on the sensor surface is recognized by an antibody and quantified electrochemically after the sugar moieties of the antibody have been labeled in-situ with ferroceneboronic acid. The sensitivity of this sensor is about threefold higher than the sensitivity of a hemoglobin sensor, where the ferroceneboronic acid is bound directly to HbA1c.},
  language  = {en}
}
@article{YarmanWollenbergerScheller2013,
  author    = {Yarman, Aysu and Wollenberger, Ursula and Scheller, Frieder W.},
  title     = {Sensors based on cytochrome P450 and CYP mimicking systems},
  series = {ELECTROCHIMICA ACTA},
  volume    = {110},
  journal   = {ELECTROCHIMICA ACTA},
  publisher = {PERGAMON-ELSEVIER SCIENCE LTD},
  address   = {OXFORD},
  issn      = {0013-4686},
  doi       = {10.1016/j.electacta.2013.03.154},
  pages     = {63 -- 72},
  year      = {2013},
  abstract  = {Cytochrome P450 enzymes (CYPs) act on more than 90 percent of all drugs currently on the market. The catalytic cycle requires electron supply to the heme iron in the presence of oxygen. Electrochemistry allows to characterise the reaction mechanism of these redox enzymes by observing the electron transfer in real time. According to the number of publications on protein electrochemistry CYP has the third position after glucose oxidase and cytochrome c. CYP based enzyme electrodes for the quantification of drugs, metabolites or pesticides have been developed using different iso-enzymes. A crucial step in the sensor development is the efficiency of coupling the biocatalytic systems with the electrode is. In the 1970s the direct electron transfer of heme and heme peptides called microperoxidases (MPs) was used as model of oxidoreductases. They exhibit a broad substrate spectrum including hydroxylation of selected aromatic substrates, demethylation and epoxidation by means of hydrogen peroxide. It overlaps with that of P450 making heme and MPs to alternate recognition elements in biosensors for the detection of typical CYP substrates. In these enzyme electrodes the signal is generated by the conversion of all substrates thus representing in complex media an overall parameter. By combining the biocatalytic substrate conversion with selective binding to a molecularly imprinted polymer layer the specificity has been improved. Here we discuss different approaches of biosensors based on CYP, microperoxidases and catalytically active MIPs and discuss their potential as recognition elements in biosensors. The performance of these sensors and their further development are discussed. (C) 2013 Elsevier Ltd. All rights reserved.},
  language  = {en}
}
@article{StoeckleinRohdeScharteetal.2000,
  author    = {St{\"o}cklein, Walter F. M. and Rohde, M. and Scharte, Gudrun and Behrsing, Olaf and Warsinke, Axel and Micheel, Burkhard and Scheller, Frieder W.},
  title     = {Sensitive detection of triazine and phenylurea pesticides in pure organic solvent by enzyme linked immunsorbent assay (ELISA): stabilities, solubilities and sensitives},
  year      = {2000},
  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{LisdatDronovMoehwaldetal.2009,
  author    = {Lisdat, Fred and Dronov, Roman and M{\"o}hwald, Helmuth and Scheller, Frieder W. and Kurth, Dirk G.},
  title     = {Self-assembly of electro-active protein architectures on electrodes for the construction of biomimetic signal chains},
  issn      = {1359-7345},
  doi       = {10.1039/B813559b},
  year      = {2009},
  abstract  = {The layer-by-layer adsorption technique based on the consecutive deposition of oppositely charged species is for the preparation of protein multilayers with fully electro-active protein molecules. The methodology was established with cytochrome c and the polyelectrolyte sulfonated polyaniline (PASA). The technique is also useful for the construction of bi-protein architectures confining protein-protein communication to an electrode. Following natural examples of protein complexes with defined signal transfer, cytochrome c was arranged with enzymes such as xanthine oxidase, bilirubin oxidase, laccase, and sulfite oxidase in self-assembled multilayer architectures. Thus, biomimetic signal chains from the enzyme substrate via the enzyme and cytochrome c towards the electrode can be established. Communication between proteins immobilised in multiple layers on the electrode can be achieved by in situ generation of small shuttle molecules or more advantageously by direct interprotein electron transfer. This allows the construction of new sensing electrodes, the properties of which can be tuned by the number of deposited protein layers. The mechanism of electron transfer within such protein assemblies on gold electrodes will be discussed.},
  language  = {en}
}
@misc{SchellerSakarDasdan2016,
  author    = {Scheller, Frieder W. and Sakar Dasdan, Dolunay},
  title     = {Selected papers presented on the 2nd International Conference on the New Trends in Chemistry, Zagreb, Croatia, April 19-22, 2016 Preface},
  series = {Bulgarian chemical communications : journal of the Chemical Institutes of the Bulgarian Academy of Sciences and of the Bulgarian Chemical Society = Izvestija po chimija},
  volume    = {48},
  journal   = {Bulgarian chemical communications : journal of the Chemical Institutes of the Bulgarian Academy of Sciences and of the Bulgarian Chemical Society = Izvestija po chimija},
  publisher = {Bulgarian Academy of Sciences},
  address   = {Sofia},
  issn      = {0324-1130},
  pages     = {4 -- 4},
  year      = {2016},
  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{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{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{BierKleinjungScheller1997,
  author    = {Bier, Frank Fabian and Kleinjung, Frank and Scheller, Frieder W.},
  title     = {Real time measurement of nucleic acid hybridization using evanescent wave sensors - step towards the genosensor},
  year      = {1997},
  language  = {en}
}
@article{WelzelKossmehlEngelmannetal.1996,
  author    = {Welzel, H.-P. and Kossmehl, G. and Engelmann, G. and Neumann, B. and Wollenberger, Ursula and Scheller, Frieder W. and Schr{\"o}der, W.},
  title     = {Reactive groups on polymer covered electrodes, 4. Lactate-oxidase-biosensor based on electrodes modifies by polyphiophene},
  year      = {1996},
  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{LisdatScheller2000,
  author    = {Lisdat, Fred and Scheller, Frieder W.},
  title     = {Principles of sensorial radical detection - a minireview},
  year      = {2000},
  language  = {en}
}
@article{SchellerSchubertFederowitz1997,
  author    = {Scheller, Frieder W. and Schubert, Frank and Federowitz, J.},
  title     = {Present state and frontiers in biosensorics},
  year      = {1997},
  language  = {en}
}
@article{SchellerHeiduschka1994,
  author    = {Scheller, Frieder W. and Heiduschka, P.},
  title     = {Preparation of an electrode surface with a high density of binding sites by an electrochemical reduction of a poly (nitrophenol) film},
  year      = {1994},
  language  = {en}
}
@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{GhindilisMakowerScheller1995,
  author    = {Ghindilis, A. L. and Makower, Alexander and Scheller, Frieder W.},
  title     = {Potentiometric enzyme electrodes based on substrate recycling and mediatorless bioelectrocatalysis},
  year      = {1995},
  language  = {en}
}
@article{HalamekMakowerKnoescheetal.2005,
  author    = {Halamek, Jan and Makower, Alexander and Kn{\"o}sche, Kristina and Skladal, Petr and Scheller, Frieder W.},
  title     = {Piezoelectric affinity sensors for cocaine and cholinesterase inhibitors},
  year      = {2005},
  abstract  = {We report here the development of piezoelectric affinity sensors for cocaine and cholinesterase inhibitors based on the formation of affinity complexes between an immobilized cocaine derivative and an anti-cocaine antibody or cholinesterase. For both binding reactions benzoylecgonine-1,8-diamino-3,4-dioxaoctane (BZE-DADOO) was immobilized on the surface of the sensor. For immobilization. pre-conjugated BZE-DADOO with 11-mercaptomonoundecanoic acid (MUA) via 2- (5-norbornen-2,3-dicarboximide)-1,1,3,3-tetramethyluronium-tetrafluoro borate (TNTU) allowed the formation of a chemisorbed monolayer on the piezosensor surface. The detection of cocaine was based oil a competitive assay. The change of frequency measured after 300 s of the binding reaction was used as the signal. The maximum binding of the antibody resulted in a frequency decrease of 35 Hz (with an imprecision 3\%, n = 3) while the presence of 100 pmol I-1 cocaine decreased the binding by 11\%. The limit of detection was consequently below 100 pmol I-1 for cocaine. The total time of one analysis was 15 min. This BZE-DADOO-modified sensor was adapted for the detection of organophosphates. BZE-DADOO - a competitive inhibitor - served as binding element for cholinesterase in a competitive assay. (C) 2004 Elsevier B.V. All rights reserved},
  language  = {en}
}
@article{BognarSupalaYarmanetal.2022,
  author    = {Bogn{\´a}r, Zs{\´o}fia and Supala, Eszter and Yarman, Aysu and Zhang, Xiaorong and Bier, Frank Fabian and Scheller, Frieder W. and Gyurcsanyi, R{\´o}bert E.},
  title     = {Peptide epitope-imprinted polymer microarrays for selective protein recognition},
  series = {Chemical science / RSC, Royal Society of Chemistry},
  volume    = {13},
  journal   = {Chemical science / RSC, Royal Society of Chemistry},
  number    = {5},
  publisher = {Royal Society of Chemistry},
  address   = {Cambridge},
  issn      = {2041-6539},
  doi       = {10.1039/d1sc04502d},
  pages     = {1263 -- 1269},
  year      = {2022},
  abstract  = {We introduce a practically generic approach for the generation of epitope-imprinted polymer-based microarrays for protein recognition on surface plasmon resonance imaging (SPRi) chips. The SPRi platform allows the subsequent rapid screening of target binding kinetics in a multiplexed and label-free manner. The versatility of such microarrays, both as synthetic and screening platform, is demonstrated through developing highly affine molecularly imprinted polymers (MIPs) for the recognition of the receptor binding domain (RBD) of SARS-CoV-2 spike protein. A characteristic nonapeptide GFNCYFPLQ from the RBD and other control peptides were microspotted onto gold SPRi chips followed by the electrosynthesis of a polyscopoletin nanofilm to generate in one step MIP arrays. A single chip screening of essential synthesis parameters, including the surface density of the template peptide and its sequence led to MIPs with dissociation constants (K-D) in the lower nanomolar range for RBD, which exceeds the affinity of RBD for its natural target, angiotensin-convertase 2 enzyme. Remarkably, the same MIPs bound SARS-CoV-2 virus like particles with even higher affinity along with excellent discrimination of influenza A (H3N2) virus. While MIPs prepared with a truncated heptapeptide template GFNCYFP showed only a slightly decreased affinity for RBD, a single mismatch in the amino acid sequence of the template, i.e. the substitution of the central cysteine with a serine, fully suppressed the RBD binding.},
  language  = {en}
}