@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{PengYarmanJetzschmannetal.2016,
  author    = {Peng, Lei and Yarman, Aysu and Jetzschmann, Katharina J. and Jeoung, Jae-Hun and Schad, Daniel and Dobbek, Holger and Wollenberger, Ursula and Scheller, Frieder W.},
  title     = {Molecularly Imprinted Electropolymer for a Hexameric Heme Protein with Direct Electron Transfer and Peroxide Electrocatalysis},
  series = {SENSORS},
  volume    = {16},
  journal   = {SENSORS},
  publisher = {MDPI},
  address   = {Basel},
  issn      = {1424-8220},
  doi       = {10.3390/s16030272},
  pages     = {1343 -- 1364},
  year      = {2016},
  abstract  = {For the first time a molecularly imprinted polymer (MIP) with direct electron transfer (DET) and bioelectrocatalytic activity of the target protein is presented. Thin films of MIPs for the recognition of a hexameric tyrosine-coordinated heme protein (HTHP) have been prepared by electropolymerization of scopoletin after oriented assembly of HTHP on a self-assembled monolayer (SAM) of mercaptoundecanoic acid (MUA) on gold electrodes. Cavities which should resemble the shape and size of HTHP were formed by template removal. Rebinding of the target protein sums up the recognition by non-covalent interactions between the protein and the MIP with the electrostatic attraction of the protein by the SAM. HTHP bound to the MIP exhibits quasi-reversible DET which is reflected by a pair of well pronounced redox peaks in the cyclic voltammograms (CVs) with a formal potential of -184.4 +/- 13.7 mV vs. Ag/AgCl (1 M KCl) at pH 8.0 and it was able to catalyze the cathodic reduction of peroxide. At saturation the MIP films show a 12-fold higher electroactive surface concentration of HTHP than the non-imprinted polymer (NIP).},
  language  = {en}
}
@misc{ErdossyHorvathYarmanetal.2016,
  author    = {Erdossy, Julia and Horvath, Viola and Yarman, Aysu and Scheller, Frieder W. and Gyurcsanyi, Robert E.},
  title     = {Electrosynthesized molecularly imprinted polymers for protein recognition},
  series = {Trends in Analytical Chemistry},
  volume    = {79},
  journal   = {Trends in Analytical Chemistry},
  publisher = {Elsevier},
  address   = {Oxford},
  issn      = {0165-9936},
  doi       = {10.1016/j.trac.2015.12.018},
  pages     = {179 -- 190},
  year      = {2016},
  abstract  = {Molecularly imprinted polymers (MIPs) for the recognition of proteins are expected to possess high affinity through the establishment of multiple interactions between the polymer matrix and the large number of functional groups of the target. However, while highly affine recognition sites need building blocks rich in complementary functionalities to their target, such units are likely to generate high levels of nonspecific binding. This paradox, that nature solved by evolution for biological receptors, needs to be addressed by the implementation of new concepts in molecular imprinting of proteins. Additionally, the structural variability, large size and incompatibility with a range of monomers made the development of protein MIPs to take a slow start. While the majority of MIP preparation methods are variants of chemical polymerization, the polymerization of electroactive functional monomers emerged as a particularly advantageous approach for chemical sensing application. Electropolymerization can be performed from aqueous solutions to preserve the natural conformation of the protein templates, with high spatial resolution and electrochemical control of the polymerization process. This review compiles the latest results, identifying major trends and providing an outlook on the perspectives of electrosynthesised protein-imprinted MIPs for chemical sensing. (C) 2016 Elsevier B.V. All rights reserved.},
  language  = {en}
}
@misc{MengerYarmanErdoessyetal.2016,
  author    = {Menger, Marcus and Yarman, Aysu and Erd{\"o}ssy, J{\´u}lia and Yildiz, Huseyin Bekir and Gyurcs{\´a}nyi, R{\´o}bert E. and Scheller, Frieder W.},
  title     = {MIPs and Aptamers for Recognition of Proteins in Biomimetic Sensing},
  series = {Biosensors : open access journal},
  volume    = {6},
  journal   = {Biosensors : open access journal},
  publisher = {MDPI},
  address   = {Basel},
  issn      = {2079-6374},
  doi       = {10.3390/bios6030035},
  pages     = {4399 -- 4413},
  year      = {2016},
  abstract  = {Biomimetic binders and catalysts have been generated in order to substitute the biological pendants in separation techniques and bioanalysis. The two major approaches use either "evolution in the test tube" of nucleotides for the preparation of aptamers or total chemical synthesis for molecularly imprinted polymers (MIPs). The reproducible production of aptamers is a clear advantage, whilst the preparation of MIPs typically leads to a population of polymers with different binding sites. The realization of binding sites in the total bulk of the MIPs results in a higher binding capacity, however, on the expense of the accessibility and exchange rate. Furthermore, the readout of the bound analyte is easier for aptamers since the integration of signal generating labels is well established. On the other hand, the overall negative charge of the nucleotides makes aptamers prone to non-specific adsorption of positively charged constituents of the sample and the "biological" degradation of non-modified aptamers and ionic strength-dependent changes of conformation may be challenging in some application.},
  language  = {en}
}
@article{YarmanScheller2016,
  author    = {Yarman, Aysu and Scheller, Frieder W.},
  title     = {MIP-esterase/Tyrosinase Combinations for Paracetamol and Phenacetin},
  series = {Electroanalysis : an international journal devoted to fundamental and practical aspects of electroanalysis},
  volume    = {28},
  journal   = {Electroanalysis : an international journal devoted to fundamental and practical aspects of electroanalysis},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1040-0397},
  doi       = {10.1002/elan.201600042},
  pages     = {2222 -- 2227},
  year      = {2016},
  abstract  = {A new electrochemical MIP sensor for the most frequently used drug paracetamol (PAR) was prepared by electropolymerization of mixtures containing the template molecule and the functional monomers ophenylenediamine, resorcinol and aniline. The imprinting factor of 12 reflects the effective target binding to the MIP as compared with the non-imprinted electropolymer. Combination of the MIP with a nonspecific esterase allows the measurement of phenacetin - another analgesic drug. In the second approach the PAR containing sample solution was pretreated with tyrosinase in order to prevent electrochemical interferences by ascorbic acid and uric acid. Interference-free indication at a very low electrode potential without fouling of the electrode surface was achieved with the o-phenylenediamine: resorcinol-based MIP.},
  language  = {en}
}
@misc{PengYarmanJetzschmannetal.2017,
  author    = {Peng, Lei and Yarman, Aysu and Jetzschmann, Katharina J. and Jeoung, Jae-Hun and Schad, Daniel and Dobbek, Holger and Wollenberger, Ursula and Scheller, Frieder W.},
  title     = {Molecularly imprinted electropolymer for a hexameric heme protein with direct electron transfer and peroxide electrocatalysis},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-400627},
  pages     = {11},
  year      = {2017},
  abstract  = {For the first time a molecularly imprinted polymer (MIP) with direct electron transfer (DET) and bioelectrocatalytic activity of the target protein is presented. Thin films of MIPs for the recognition of a hexameric tyrosine-coordinated heme protein (HTHP) have been prepared by electropolymerization of scopoletin after oriented assembly of HTHP on a self-assembled monolayer (SAM) of mercaptoundecanoic acid (MUA) on gold electrodes. Cavities which should resemble the shape and size of HTHP were formed by template removal. Rebinding of the target protein sums up the recognition by non-covalent interactions between the protein and the MIP with the electrostatic attraction of the protein by the SAM. HTHP bound to the MIP exhibits quasi-reversible DET which is reflected by a pair of well pronounced redox peaks in the cyclic voltammograms (CVs) with a formal potential of -184.4 ± 13.7 mV vs. Ag/AgCl (1 M KCl) at pH 8.0 and it was able to catalyze the cathodic reduction of peroxide. At saturation the MIP films show a 12-fold higher electroactive surface concentration of HTHP than the non-imprinted polymer (NIP).},
  language  = {en}
}
@misc{MengerYarmanErdőssyetal.2017,
  author    = {Menger, Marcus and Yarman, Aysu and Erdőssy, J{\´u}lia and Yildiz, Huseyin Bekir and Gyurcs{\´a}nyi, R{\´o}bert E. and Scheller, Frieder W.},
  title     = {MIPs and aptamers for recognition of proteins in biomimetic sensing},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-400496},
  pages     = {19},
  year      = {2017},
  abstract  = {Biomimetic binders and catalysts have been generated in order to substitute the biological pendants in separation techniques and bioanalysis. The two major approaches use either "evolution in the test tube" of nucleotides for the preparation of aptamers or total chemical synthesis for molecularly imprinted polymers (MIPs). The reproducible production of aptamers is a clear advantage, whilst the preparation of MIPs typically leads to a population of polymers with different binding sites. The realization of binding sites in the total bulk of the MIPs results in a higher binding capacity, however, on the expense of the accessibility and exchange rate. Furthermore, the readout of the bound analyte is easier for aptamers since the integration of signal generating labels is well established. On the other hand, the overall negative charge of the nucleotides makes aptamers prone to non-specific adsorption of positively charged constituents of the sample and the "biological" degradation of non-modified aptamers and ionic strength-dependent changes of conformation may be challenging in some application.},
  language  = {en}
}
@misc{YarmanDechtriratBosserdtetal.2015,
  author    = {Yarman, Aysu and Dechtrirat, Decha and Bosserdt, Maria and Jetzschmann, Katharina J. and Gajovic-Eichelmann, Nenad and Scheller, Frieder W.},
  title     = {Cytochrome c-derived hybrid systems based on moleculary imprinted polymers},
  series = {Electroanalysis : an international journal devoted to fundamental and practical aspects of electroanalysis},
  volume    = {27},
  journal   = {Electroanalysis : an international journal devoted to fundamental and practical aspects of electroanalysis},
  number    = {3},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1040-0397},
  doi       = {10.1002/elan.201400592},
  pages     = {573 -- 586},
  year      = {2015},
  abstract  = {Hybrid architectures which combine a MIP with an immobilized affinity ligand or a biocatalyst sum up the advantages of both components. In this paper, hybrid architectures combining a layer of a molecularly imprinted electropolymer with a mini-enzyme or a self-assembled monolayer will be presented. (i) Microperoxidase-11 (MP-11) catalyzed oxidation of the drug aminopyrine on a product-imprinted sublayer: The peroxide dependent conversion of the analyte aminopyrine takes place in the MP-11 containing layer on top of a product-imprinted electropolymer on the indicator electrode. The hierarchical architecture resulted in the elimination of interfering signals for ascorbic acid and uric acid. An advantage of the new hierarchical structure is the separation of MIP formation by electropolymerization and immobilization of the catalyst. In this way it was for the first time possible to integrate an enzyme with a MIP layer in a sensor configuration. This combination has the potential to be transferred to other enzymes, e.g. P450, opening the way to clinically important analytes. (ii) Epitope-imprinted poly-scopoletin layer for binding of the C-terminal peptide and cytochrome c (Cyt c): The MIP binds both the target peptide and the parent protein almost eight times stronger than the non-imprinted polymer with affinities in the lower micromolar range. Exchange of only one amino acid in the peptide decreases the binding by a factor of five. (iii) MUA-poly-scopoletin MIP for cytochrome c: Cyt c bound to the MIP covered gold electrode exhibits direct electron transfer with a redox potential and rate constant typical for the native protein. The MIP cover layer suppresses the displacement of the target protein by BSA or myoglobin. The combination of protein imprinted polymers with an efficient electron transfer is a new concept for characterizing electroactive proteins such as Cyt c. The competition with other proteins shows that the MIP binds its target Cyt c preferentially and that molecular shape and the charge of protein determine the binding of interfering proteins.},
  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{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{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}
}
@article{TanneJeoungPengetal.2015,
  author    = {Tanne, Johannes and Jeoung, Jae-Hun and Peng, Lei and Yarman, Aysu and Dietzel, Birgit and Schulz, Burkhard and Schad, Daniel and Dobbek, Holger and Wollenberger, Ursula and Bier, Frank Fabian and Scheller, Frieder W.},
  title     = {Direct Electron Transfer and Bioelectrocatalysis by a Hexameric, Heme Protein at Nanostructured Electrodes},
  series = {Electroanalysis : an international journal devoted to fundamental and practical aspects of electroanalysis},
  volume    = {27},
  journal   = {Electroanalysis : an international journal devoted to fundamental and practical aspects of electroanalysis},
  number    = {10},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1040-0397},
  doi       = {10.1002/elan.201500231},
  pages     = {2262 -- 2267},
  year      = {2015},
  abstract  = {A nanohybrid consisting of poly(3-aminobenzenesulfonic acid-co-aniline) and multiwalled carbon nanotubes [MWCNT-P(ABS-A)]) on a gold electrode was used to immobilize the hexameric tyrosine-coordinated heme protein (HTHP). The enzyme showed direct electron transfer between the heme group of the protein and the nanostructured surface. Desorption of the noncovalently bound heme from the protein could be excluded by control measurements with adsorbed hemin on aminohexanthiol-modified electrodes. The nanostructuring and the optimised charge characteristics resulted in a higher protein coverage as compared with MUA/MU modified electrodes. The adsorbed enzyme shows catalytic activity for the cathodic H2O2 reduction and oxidation of NADH.},
  language  = {en}
}
@article{SchellerYarmanBachmannetal.2014,
  author    = {Scheller, Frieder W. and Yarman, Aysu and Bachmann, Till and Hirsch, Thomas and Kubick, Stefan and Renneberg, Reinhard and Schumacher, Soeren and Wollenberger, Ursula and Teller, Carsten and Bier, Frank Fabian},
  title     = {Future of biosensors: a personal view},
  series = {Advances in biochemical engineering, biotechnology},
  volume    = {140},
  journal   = {Advances in biochemical engineering, biotechnology},
  editor    = {Gu, MB and Kim, HS},
  publisher = {Springer},
  address   = {Berlin},
  isbn      = {978-3-642-54143-8; 978-3-642-54142-1},
  issn      = {0724-6145},
  doi       = {10.1007/10_2013_251},
  pages     = {1 -- 28},
  year      = {2014},
  abstract  = {Biosensors representing the technological counterpart of living senses have found routine application in amperometric enzyme electrodes for decentralized blood glucose measurement, interaction analysis by surface plasmon resonance in drug development, and to some extent DNA chips for expression analysis and enzyme polymorphisms. These technologies have already reached a highly advanced level and need minor improvement at most. The dream of the "100-dollar' personal genome may come true in the next few years provided that the technological hurdles of nanopore technology or of polymerase-based single molecule sequencing can be overcome. Tailor-made recognition elements for biosensors including membrane-bound enzymes and receptors will be prepared by cell-free protein synthesis. As alternatives for biological recognition elements, molecularly imprinted polymers (MIPs) have been created. They have the potential to substitute antibodies in biosensors and biochips for the measurement of low-molecular-weight substances, proteins, viruses, and living cells. They are more stable than proteins and can be produced in large amounts by chemical synthesis. Integration of nanomaterials, especially of graphene, could lead to new miniaturized biosensors with high sensitivity and ultrafast response. In the future individual therapy will include genetic profiling of isoenzymes and polymorphic forms of drug-metabolizing enzymes especially of the cytochrome P450 family. For defining the pharmacokinetics including the clearance of a given genotype enzyme electrodes will be a useful tool. For decentralized online patient control or the integration into everyday "consumables' such as drinking water, foods, hygienic articles, clothing, or for control of air conditioners in buildings and cars and swimming pools, a new generation of "autonomous' biosensors will emerge.},
  language  = {en}
}
@article{NeumannYarmanWollenbergeretal.2014,
  author    = {Neumann, Bettina and Yarman, Aysu and Wollenberger, Ursula and Scheller, Frieder W.},
  title     = {Characterization of the enhanced peroxidatic activity of amyloid beta peptide-hemin complexes towards neurotransmitters},
  series = {Analytical \& bioanalytical chemistry},
  volume    = {406},
  journal   = {Analytical \& bioanalytical chemistry},
  number    = {14},
  publisher = {Springer},
  address   = {Heidelberg},
  issn      = {1618-2642},
  doi       = {10.1007/s00216-014-7822-8},
  pages     = {3359 -- 3364},
  year      = {2014},
  abstract  = {Binding of heme to the amyloid peptides A beta 40/42 is thought to be an initial step in the development of symptoms in the early stages of Alzheimer's disease by enhancing the intrinsic peroxidatic activity of heme. We found considerably higher acceleration of the reaction for the physiologically relevant neurotransmitters dopamine and serotonin than reported earlier for the artificial substrate 3,3',5,5'-tetramethylbenzidine (TMB). Thus, the binding of hemin to A beta peptides might play an even more crucial role in the early stages of Alzheimer's disease than deduced from these earlier results. To mimic complex formation, a new surface architecture has been developed: The interaction between the truncated amyloid peptide A beta 1-16 and hemin immobilized on an aminohexanethiol spacer on a gold electrode has been analyzed by cyclic voltammetry. The resulting complex has a redox pair with a 25 mV more cathodic formal potential than hemin alone.},
  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}
}
@article{DechtriratGajovicEichelmannWojciketal.2014,
  author    = {Dechtrirat, Decha and Gajovic-Eichelmann, Nenad and Wojcik, Felix and Hartmann, Laura and Bier, Frank Fabian and Scheller, Frieder W.},
  title     = {Electrochemical displacement sensor based on ferrocene boronic acid tracer and immobilized glycan for saccharide binding proteins and E. coli},
  series = {Biosensors and bioelectronics : the principal international journal devoted to research, design development and application of biosensors and bioelectronics},
  volume    = {58},
  journal   = {Biosensors and bioelectronics : the principal international journal devoted to research, design development and application of biosensors and bioelectronics},
  publisher = {Elsevier},
  address   = {Oxford},
  issn      = {0956-5663},
  doi       = {10.1016/j.bios.2014.02.028},
  pages     = {1 -- 8},
  year      = {2014},
  abstract  = {Pathogens such as viruses and bacteria use their envelope proteins and their adhesin lectins to recognize the glycan residues presented on the cell surface of the target tissues. This principle of recognition is used in a new electrochemical displacement sensor for the protein concanavalin A (ConA). A gold electrode was first modified with a self-assembled monolayer of a thiolated mannose/OEG conjugate and a ferrocene boroxol derivative was pre-assembled as reporter molecule onto the mannose surface. The novel tracer molecule based on a 2-hydroxymethyl phenyl boronic acid derivative binds even at neutral pH to the saccharides which could expand the application towards biological samples (i.e., urine and feces). Upon the binding of ConA, the tracer was displaced and washed away from the sensor surface leading to a decrease in the electrochemical signal. Using square wave voltammetry (SWV), the concentration of ConA in the sample solution could be determined in the dynamic concentration range established from 38 nmol L-1 to 5.76 mu mol L-1 with a reproducible detection limit of 1 mu g mL(-1) (38 nmol L-1) based on the signal-to-noise ratio (S/N=3) with fast response of 15 min. The new reporter molecule showed a reduced non-specific displacement by BSA and ribonuclease A. The sensor was also successfully transferred to the first proof of principle for the detection of Escherichia coli exhibiting a detection limit of approximately 6 x 102 cells/mL Specificity of the displacement by target protein ConA and E. coli was demonstrated since the control proteins (i.e., BSA and RNaseA) and the control E. coli strain, which lack of type 1 fimbriae, were ineffective. (C) 2014 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{YarmanBadalyanGajovicEichelmannetal.2011,
  author    = {Yarman, Aysu and Badalyan, Artavazd and Gajovic-Eichelmann, Nenad and Wollenberger, Ursula and Scheller, Frieder W.},
  title     = {Enzyme electrode for aromatic compounds exploiting the catalytic activities of microperoxidase-11},
  series = {Biosensors and bioelectronics : the principal international journal devoted to research, design development and application of biosensors and bioelectronics},
  volume    = {30},
  journal   = {Biosensors and bioelectronics : the principal international journal devoted to research, design development and application of biosensors and bioelectronics},
  number    = {1},
  publisher = {Elsevier},
  address   = {Oxford},
  issn      = {0956-5663},
  doi       = {10.1016/j.bios.2011.09.004},
  pages     = {320 -- 323},
  year      = {2011},
  abstract  = {Microperoxidase-11 (MR-11) which has been immobilised in a matrix of chitosan-embedded gold nanoparticles on the surface of a glassy carbon electrode catalyzes the conversion of aromatic substances. This peroxide-dependent catalysis of microperoxidase has been applied in an enzyme electrode for the first time to indicate aromatic compounds such as aniline. 4-fluoroaniline, catechol and p-aminophenol. The electrode signal is generated by the cathodic reduction of the quinone or quinoneimine which is formed in the presence of both MP-II and peroxide from the substrate. The same sensor principle will be extended to aromatic drugs.},
  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{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{BosserdtGajovicEichelmanScheller2013,
  author    = {Bosserdt, Maria and Gajovic-Eichelman, Nenad and Scheller, Frieder W.},
  title     = {Modulation of direct electron transfer of cytochrome c by use of a molecularly imprinted thin film},
  series = {Analytical \& bioanalytical chemistry},
  volume    = {405},
  journal   = {Analytical \& bioanalytical chemistry},
  number    = {20},
  publisher = {Springer},
  address   = {Heidelberg},
  issn      = {1618-2642},
  doi       = {10.1007/s00216-013-7009-8},
  pages     = {6437 -- 6444},
  year      = {2013},
  abstract  = {We describe the preparation of a molecularly imprinted polymer film (MIP) on top of a self-assembled monolayer (SAM) of mercaptoundecanoic acid (MUA) on gold, where the template cytochrome c (cyt c) participates in direct electron transfer (DET) with the underlying electrode. To enable DET, a non-conductive polymer film is electrodeposited from an aqueous solution of scopoletin and cyt c on to the surface of a gold electrode previously modified with MUA. The electroactive surface concentration of cyt c was 0.5 pmol cm(-2). In the absence of the MUA layer, no cyt c DET was observed and the pseudo-peroxidatic activity of the scopoletin-entrapped protein, assessed via oxidation of Ampliflu red in the presence of hydrogen peroxide, was only 30 \% of that for the MIP on MUA. This result indicates that electrostatic adsorption of cyt c by the MUA-SAM substantially increases the surface concentration of cyt c during the electrodeposition step, and is a prerequisite for the productive orientation required for DET. After template removal by treatment with sulfuric acid, rebinding of cyt c to the MUA-MIP-modified electrode occurred with an affinity constant of 100,000 mol(-1) L, a value three times higher than that determined by use of fluorescence titration for the interaction between scopoletin and cyt c in solution. The DET of cyt c in the presence of myoglobin, lysozyme, and bovine serum albumin (BSA) reveals that the MIP layer suppresses the effect of competing proteins.},
  language  = {en}
}
@article{YarmanScheller2013,
  author    = {Yarman, Aysu and Scheller, Frieder W.},
  title     = {Coupling biocatalysis with molecular imprinting in a biomimetic sensor},
  series = {Angewandte Chemie : a journal of the Gesellschaft Deutscher Chemiker ; International edition},
  volume    = {52},
  journal   = {Angewandte Chemie : a journal of the Gesellschaft Deutscher Chemiker ; International edition},
  number    = {44},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1433-7851},
  doi       = {10.1002/anie.201305368},
  pages     = {11521 -- 11525},
  year      = {2013},
  language  = {en}
}
@article{FrascavonGrabergFengetal.2010,
  author    = {Frasca, Stefano and von Graberg, Till and Feng, Jiu-Ju and Thomas, Arne and Smarsly, Bernd M. and Weidinger, Inez M. and Scheller, Frieder W. and Hildebrandt, Peter and Wollenberger, Ursula},
  title     = {Mesoporous indium tin oxide as a novel platform for bioelectronics},
  issn      = {1867-3880},
  doi       = {10.1002/cctc.201000047},
  year      = {2010},
  abstract  = {Stable immobilization and reversible electrochemistry of cytochrome c in a tranparent indium tin oxide film with a well-defined mesoporosity (mpITO) is demonstrated. the transparency and good conductivity, in combination with the large surface area of mpITO, allow the incorporation of a high amount of elelctroactive biomolecules and their electrochemical and spectroscopic investigation. UV/Vis and resonance Raman spectroscopy, in combination with direct protein voltammetry are employed for the characterization of cytochrome c immobilized in the mpITO and reveal no perturbant of the structural of the integrity of the redox protein. The potential of this modified material as a biosensor detection of superoxide anions is also demonstrated.},
  language  = {en}
}
@article{BaeumnerGauglitzScheller2010,
  author    = {Baeumner, Antje J. and Gauglitz, Guenter and Scheller, Frieder W.},
  title     = {Focus on bioanalysis},
  issn      = {1618-2642},
  doi       = {10.1007/s00216-010-4203-9},
  year      = {2010},
  abstract  = {Editoria},
  language  = {en}
}
@article{SpricigoDronovLisdatetal.2009,
  author    = {Spricigo, Roberto and Dronov, Roman and Lisdat, Fred and Leimk{\"u}hler, Silke and Scheller, Frieder W. and Wollenberger, Ursula},
  title     = {Electrocatalytic sulfite biosensor with human sulfite oxidase co-immobilized with cytochrome c in a polyelectrolyte-containing multilayer},
  issn      = {1618-2642},
  doi       = {10.1007/s00216-008-2432-y},
  year      = {2009},
  abstract  = {An efficient electrocatalytic biosensor for sulfite detection was developed by co-immobilizing sulfite oxidase and cytochrome c with polyaniline sulfonic acid in a layer-by-layer assembly. QCM, UV-Vis spectroscopy and cyclic voltammetry revealed increasing loading of electrochemically active protein with the formation of multilayers. The sensor operates reagentless at low working potential. A catalytic oxidation current was detected in the presence of sulfite at the modified gold electrode, polarized at +0.1 V ( vs. Ag/AgCl 1 M KCl). The stability of the biosensor performance was characterized and optimized. A 17-bilayer electrode has a linear range between 1 and 60 mu M sulfite with a sensitivity of 2.19 mA M-1 sulfite and a response time of 2 min. The electrode retained a stable response for 3 days with a serial reproducibility of 3.8\% and lost 20\% of sensitivity after 5 days of operation. It is possible to store the sensor in a dry state for more than 2 months. The multilayer electrode was used for determination of sulfite in unspiked and spiked samples of red and white wine. The recovery and the specificity of the signals were evaluated for each sample.},
  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{LoewWollenbergerSchelleretal.2009,
  author    = {Loew, Noya and Wollenberger, Ursula and Scheller, Frieder W. and Katterle, Martin},
  title     = {Direct electrochemistry and spectroelectrochemistry of osmium substituted horseradish peroxidase},
  issn      = {1567-5394},
  doi       = {10.1016/j.bioelechem.2009.03.015},
  year      = {2009},
  abstract  = {In this contribution the substitution of the central protoporphyrin IX iron complex of horseradish peroxidase by the respective osmium porphyrin complex is described. The direct electrochemical reduction of the Os containing horseradish peroxidase (OsHRP) was achieved at ITO and modified glassy carbon electrodes and in combination with spectroscopy revealed the three redox couples (OsHRP)-H-III/(OsHRP)-H-IV, (OsHRP)-H-IV/(OsHRP)-H-V and (OsHRP)-H-V/ (OsHRP)-H-VI. The midpoint potentials differ dependent on the electrode material used with E-1/2 (Os-III/IV) of -0.4 V (ITO) and -0.25 V (GC), E-1/2 (Os-IV/V) of -0.16 V (ITO) and +0.10 V (GC), and E-1/2 (Os-V/VI)of +018 V (ITO), respectively Moreover, with immobilised OsHRP the direct electrocatalytic reduction of hydrogen peroxide and tert-butyl hydroperoxide was observed. In comparison to electrodes modified with native HRP the sensitivity of the OsHRP-electrode for tert-butyl hydroperoxide is higher.},
  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}
}
@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{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{HalamekWollenbergerStoeckleinetal.2007,
  author    = {Hal{\´a}mek, Jan and Wollenberger, Ursula and St{\"o}cklein, Walter F. M. and Scheller, Frieder W.},
  title     = {Development of a biosensor for glycated hemoglobin},
  issn      = {0013-4686},
  doi       = {10.1016/j.electacta.2007.03.059},
  year      = {2007},
  abstract  = {The development of an electrochemical piezoelectric sensor for the detection of glycated hemoglobin is presented. The total hemoglobin (Hb) content is monitored with a mass-sensitive quartz crystal modified with surfactants, and the glycated fraction of the immobilized Hb is determined by subsequent voltarnmetric measurement of the coupled ferroceneboronic acid. Different modifications of the sensor were tested for their hemoglobin binding ability. Deoxycholate (DOCA) was found to be the most suitable among the examined modifiers. Piezoelectric quartz crystals with gold electrodes were modified with DOCA by covalent binding to a pre-formatted 4-aminothiophenol monolayer. The properties of the Hb binding to DOCA and the pH effect on this interaction were studied. In the proposed assay for glycated hemoglobin at first an Hb sample is incubated with ferroceneboronic acid (FcBA), which binds to the fructosyl residue of the glycated Hb. Then this preincubated Hb sample is allowed to interact with the DOCA-modified piezoelectric quartz crystal. The binding is monitored by quartz crystal nanobalance QCN). The amount of FcBA present on the sensor surface is determined by square wave voltammetry. The binding of FcBA results in well-defined peaks with an EO' of +200 mV versus Ag/AgC1 (1 M KC1). The peak height depends on the degree of glycated Hb in the sample ranging from 0\% to 20\% of total Hb. The regeneration of the sensing surface is achieved by pepsin digestion of the deposited Hb. Thus the sensor can be re-used more than 30 times.},
  language  = {en}
}
@article{ShumyantsevaIvanovBistolasetal.2004,
  author    = {Shumyantseva, V. V. and Ivanov, Y. D. and Bistolas, Nikitas and Scheller, Frieder W. and Archakov, Alexander I. and Wollenberger, Ursula},
  title     = {Direct electron transfer of cytochrome P450 2B4 at electrodes modified with non-ionic detergent and colloidal clay nanoparticles},
  year      = {2004},
  abstract  = {A method for construction of biosensors with membranous cytochrome P450 isoenzymes was developed based on clay/ detergent/protein mixed films. Thin films of sodium montmorillonite colloid with incorporated cytochrome P450 2134 (CYP2B4) with nonionic detergent were prepared on glassy carbon electrodes. The modified electrodes were electrochemically characterized, and bio-electrocatalytic reactions were followed. CYP2B4 can be reduced fast on clay- modified glassy carbon electrodes in the presence of the nonionic detergent Tween 80. In anaerobic solutions, reversible oxidation and reduction is obtained with a formal potential between -0.292 and - 0.305 V vs Ag/AgCl 1 M KCl depending on the preparation of the biosensor. In air-saturated solution, bio-electrocatalytic reduction currents can be obtained with the CYP2B4-modified electrode on addition of typical substrates such as aminopyrine and benzphetamine. This reaction was suppressed when methyrapone, an inhibitor of P450 reactions, was present. Measurement of product formation also indicates the bioelectrocatialysis by CYP2B4},
  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{SchellerKirsteinSchubertetal.1993,
  author    = {Scheller, Frieder W. and Kirstein, Dieter and Schubert, Florian and Pfeiffer, Dorothea and McNeil, C. J.},
  title     = {Enzymes in electrochemical biosensors},
  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}
}
@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{PfeifferSchellerSchubertetal.1993,
  author    = {Pfeiffer, Dorothea and Scheller, Frieder W. and Schubert, Florian and Setz, K.},
  title     = {Amperometric enzyme electrodes for lactate and glucose determinations in highly diluted and undiluted media},
  year      = {1993},
  language  = {en}
}
@article{SchellerWollenbergerSchubertetal.1993,
  author    = {Scheller, Frieder W. and Wollenberger, Ursula and Schubert, Florian and Pfeiffer, Dorothea and Markower, Alexander and McNeil, C. J.},
  title     = {Multienzyme biosensors : coupled enzyme reactions and enzyme activation},
  year      = {1993},
  language  = {en}
}
@article{BogdanovskayaFridmanTarasevichetal.1994,
  author    = {Bogdanovskaya, V. A. and Fridman, Vadim and Tarasevich, M. R. and Scheller, Frieder W.},
  title     = {Bioelectrocatalysis by immobilized peroxidase : the reaction mechanism and the possibility of electroanalytical detection of both inhibitors and activators of enzyme},
  year      = {1994},
  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{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{SchellerMakowerGhindilisetal.1995,
  author    = {Scheller, Frieder W. and Makower, Alexander and Ghindilis, A. L. and Bier, Frank Fabian and Ehrentreich-F{\"o}rster, Eva and Wollenberger, Ursula and Bauer, Christian G. and Micheel, Burkhard and Pfeiffer, Dorothea and Szeponik, Jan and Michael, N. and Kaden, H.},
  title     = {Enzyme sensors for subnanomolar concentrations},
  year      = {1995},
  language  = {en}
}
@article{StancikMacholanPluhaceketal.1995,
  author    = {Stanc{\´i}k, L. and Machol{\´a}n, L. and Pluhacek, I. and Scheller, Frieder W.},
  title     = {Biosensing of rapeseed glucosinolates using amperometric enzyme electrodes based on membrane-bound glucose oxidase or tyrosinase},
  year      = {1995},
  language  = {en}
}
@article{RiedelBeyersdorfRadeckNeumannetal.1995,
  author    = {Riedel, K. and Beyersdorf-Radeck, Baerbel and Neumann, B. and Scheller, Frieder W. and Schmid, Rolf D.},
  title     = {Microbial sensors for determination of aromatics and their chloro derivatives. Part III: Determination of chlorinated phenols using a biosensor containing Trichosporon beigelii (cutaneum)},
  year      = {1995},
  language  = {en}
}
@article{IlievKaishevaSchelleretal.1995,
  author    = {Iliev, I. and Kaisheva, A. and Scheller, Frieder W. and Pfeiffer, Dorothea},
  title     = {Amperometric gas-diffusion / enzyme electrode},
  year      = {1995},
  language  = {en}
}
@article{JinWollenbergerBieretal.1995,
  author    = {Jin, Wen and Wollenberger, Ursula and Bier, Frank Fabian and Scheller, Frieder W.},
  title     = {Construction and characterization of multi-layer-enzyme electrode : covalent binding of quinoprotein glucose dehydrogenase onto gold electrodes},
  year      = {1995},
  language  = {en}
}
@article{GhindilisMakowerBaueretal.1995,
  author    = {Ghindilis, A. L. and Makower, Alexander and Bauer, Christian G. and Bier, Frank Fabian and Scheller, Frieder W.},
  title     = {Determination of p-aminophenol and catecholamines at picomolar concentrations based on recycling enzyme amplification},
  year      = {1995},
  language  = {en}
}
@article{EremenkoMakowerJinetal.1995,
  author    = {Eremenko, A. V. and Makower, Alexander and Jin, Wen and R{\"u}ger, P. and Scheller, Frieder W.},
  title     = {Biosensor based on an enzyme modified electrode for highly - sensitive measurement of polyphenols},
  year      = {1995},
  language  = {en}
}
@article{SchellerPfeifferSchubertetal.1995,
  author    = {Scheller, Frieder W. and Pfeiffer, Dorothea and Schubert, Florian and Wollenberger, Ursula},
  title     = {Enzyme - based electrodes},
  year      = {1995},
  language  = {en}
}
@article{PfeifferSchellerMcNeiletal.1995,
  author    = {Pfeiffer, Dorothea and Scheller, Frieder W. and McNeil, C. J. and Schulmeister, Thomas},
  title     = {Cascade-like exponential substrate amplification in enzyme sensors},
  year      = {1995},
  language  = {en}
}
@article{PaeschkeHintscheWollenbergeretal.1995,
  author    = {Paeschke, Manfred and Hintsche, Rainer and Wollenberger, Ursula and Jin, Wen and Scheller, Frieder W.},
  title     = {Dynamic redox recycling of cytochrome c},
  issn      = {0022-0728},
  year      = {1995},
  language  = {en}
}
@article{WollenbergerHintscheScheller1995,
  author    = {Wollenberger, Ursula and Hintsche, R. and Scheller, Frieder W.},
  title     = {Biosensors for analytical microsystems},
  year      = {1995},
  language  = {en}
}
@article{StoeckleinSchellerAbuknesha1995,
  author    = {St{\"o}cklein, Walter F. M. and Scheller, Frieder W. and Abuknesha, Rhamadan},
  title     = {Effects of organic solvents on semicontinuous immunochemical detection of coumarin derivatives},
  year      = {1995},
  language  = {en}
}
@article{StancikMacholanScheller1995,
  author    = {Stancik, L. and Machol{\´a}n, L. and Scheller, Frieder W.},
  title     = {Biosensing of tyrosinase inhibitors in nonaqueous solvents},
  year      = {1995},
  language  = {en}
}
@article{SongBierScheller1995,
  author    = {Song, Min Ik and Bier, Frank Fabian and Scheller, Frieder W.},
  title     = {A method to detect superoxide radicals using teflon membrane and superoxide dismutase},
  year      = {1995},
  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{GhindilisMakowerScheller1995,
  author    = {Ghindilis, A. L. and Makower, Alexander and Scheller, Frieder W.},
  title     = {Nanomolar determination of the ferrocene derivatives using a recycling enzyme electrode : development of the redox label immunoassay},
  year      = {1995},
  language  = {en}
}
@article{GhindilisMakowerScheller1995,
  author    = {Ghindilis, A. L. and Makower, Alexander and Scheller, Frieder W.},
  title     = {Laccase - glucose dehydrogenase recycling enzyme electrode based on potentiometric mediatorless electrocatalytic detection},
  year      = {1995},
  language  = {en}
}
@article{GajovicWarsinkeScheller1995,
  author    = {Gajovic, Nenad and Warsinke, Axel and Scheller, Frieder W.},
  title     = {A novel multienzyme electrode for the determination of citrate},
  year      = {1995},
  language  = {en}
}
@article{EremenkoMakowerScheller1995,
  author    = {Eremenko, A. V. and Makower, Alexander and Scheller, Frieder W.},
  title     = {Measurement of nanomolar diphenols by substrate recycling coupled to a pH- sensitive electrode},
  year      = {1995},
  language  = {en}
}
@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{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{BierEhrentreichFoersterBaueretal.1996,
  author    = {Bier, Frank Fabian and Ehrentreich-F{\"o}rster, Eva and Bauer, Christian G. and Scheller, Frieder W.},
  title     = {High sensitive competitive immunodetection of 2,4-dichlorophenoxyacetic acid using enzymatic amplification with electrochemical detection},
  year      = {1996},
  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{KaishevaIlievKazarevaetal.1996,
  author    = {Kaisheva, A. and Iliev, I. and Kazareva, R. and Christov, S. and Wollenberger, Ursula and Scheller, Frieder W.},
  title     = {Enzyme/gas diffusion electrodes for determination of phenol},
  year      = {1996},
  language  = {en}
}
@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{BierEhrentreichFoersterMakoweretal.1996,
  author    = {Bier, Frank Fabian and Ehrentreich-F{\"o}rster, Eva and Makower, Alexander and Scheller, Frieder W.},
  title     = {An enzymatic amplification cycle for high sensitive immunoassay},
  year      = {1996},
  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{PfeifferSchubertWollenbergeretal.1996,
  author    = {Pfeiffer, Dorothea and Schubert, Frank and Wollenberger, Ursula and Scheller, Frieder W.},
  title     = {Electrochemical sensors : enzyme electrodes and field effect transistors},
  year      = {1996},
  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{Scheller1996,
  author    = {Scheller, Frieder W.},
  title     = {New recognition elements for bioanalytics},
  year      = {1996},
  language  = {en}
}
@article{WarsinkeBenkertScheller1996,
  author    = {Warsinke, Axel and Benkert, Alexander and Scheller, Frieder W.},
  title     = {Biomolecular modules for creatinine determination},
  year      = {1996},
  language  = {en}
}
@article{StoeckleinScheller1996,
  author    = {St{\"o}cklein, Walter F. M. and Scheller, Frieder W.},
  title     = {Laccase : a marker enzyme for solvent modified immunoassays},
  year      = {1996},
  language  = {en}
}
@article{SchellerWollenbergerPfeifferetal.1996,
  author    = {Scheller, Frieder W. and Wollenberger, Ursula and Pfeiffer, Dorothea and Schubert, Florian},
  title     = {Overview of biosensor technology : proceedings of Mosbach Symposion on Biochemical Technology},
  year      = {1996},
  language  = {en}
}
@article{BierScheller1996,
  author    = {Bier, Frank Fabian and Scheller, Frieder W.},
  title     = {Label-free observation of DNA-hybridisation and endonuclease activity on a wave guide surface using a grating coupler},
  year      = {1996},
  language  = {en}
}
@article{BierEhrentreichFoersterScheller1996,
  author    = {Bier, Frank Fabian and Ehrentreich-F{\"o}rster, Eva and Scheller, Frieder W.},
  title     = {Amplifying bienzyme cycle-linked immunoassays for determination of 2,4- dichlorphenoxyacetic acid},
  year      = {1996},
  language  = {en}
}
@article{EremenkoMakowerBaueretal.1997,
  author    = {Eremenko, A. V. and Makower, Alexander and Bauer, Christian G. and Kurochkin, I. N. and Scheller, Frieder W.},
  title     = {A bienzyme electrode for tyrosine containing peptides determination},
  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{StoeckleinScheller1997,
  author    = {St{\"o}cklein, Walter F. M. and Scheller, Frieder W.},
  title     = {Enzymes and antibodies in organic media : analytical applications},
  year      = {1997},
  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{StoeckleinWarsinkeScheller1997,
  author    = {St{\"o}cklein, Walter F. M. and Warsinke, Axel and Scheller, Frieder W.},
  title     = {Organic solvent modified enzyme-liked immunoassay for the detection of triazine herbicides},
  year      = {1997},
  language  = {en}
}
@article{GajovicWarsinkeScheller1997,
  author    = {Gajovic, Nenad and Warsinke, Axel and Scheller, Frieder W.},
  title     = {Comparsion of two enzyme sequences for a novel L-malate biosensor},
  year      = {1997},
  language  = {en}
}
@article{WelzelKossmehlEngelmannetal.1997,
  author    = {Welzel, H.-P. and Kossmehl, G. and Engelmann, G. and Neumann, B. and Wollenberger, Ursula and Scheller, Frieder W.},
  title     = {Electrochemical polymerization of functionalized thiohene derivatives for immobilization of proteins},
  year      = {1997},
  language  = {en}
}
@article{MarkowerWollenbergerHoertnageletal.1997,
  author    = {Markower, Alexander and Wollenberger, Ursula and H{\"o}rtnagel, H. and Pfeiffer, Dorothea and Scheller, Frieder W.},
  title     = {Catecholamine detection using enzymatic amplification},
  year      = {1997},
  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{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{BierEhrentreichFoersterDoellingetal.1997,
  author    = {Bier, Frank Fabian and Ehrentreich-F{\"o}rster, Eva and D{\"o}lling, R. and Eremenko, A. V. and Scheller, Frieder W.},
  title     = {A redox-label immunosensor on basis of a bi-enzyme electrode},
  year      = {1997},
  language  = {en}
}
@article{PfeifferYangSchelleretal.1997,
  author    = {Pfeiffer, Dorothea and Yang, L. and Scheller, Frieder W. and Kissinger, P. T.},
  title     = {Continous measurement of lactate in microdialysate},
  year      = {1997},
  language  = {en}
}
@article{JinWollenbergerKaergeletal.1997,
  author    = {Jin, Wen and Wollenberger, Ursula and K{\"a}rgel, E. and Schunck, W.-H. and Scheller, Frieder W.},
  title     = {Electrochemical investigation of the intermolecular electron transfer between cytochrome c and NADPH-cytochrome P450-reductase},
  year      = {1997},
  language  = {en}
}
@article{KleinjungBeierWarsinkeetal.1997,
  author    = {Kleinjung, Frank and Beier, Frank F. and Warsinke, Axel and Scheller, Frieder W.},
  title     = {Fibre-optic genosensor for specific determination of femtomolar DNA oligomers},
  year      = {1997},
  language  = {en}
}
@article{KulysDrungilieneWollenbergeretal.1997,
  author    = {Kulys, J. and Drungiliene, A. and Wollenberger, Ursula and Krikstopaitis, K. and Scheller, Frieder W.},
  title     = {Electroanalytical determination of peroxidases and laccases on carbon paste electrodes},
  year      = {1997},
  language  = {en}
}
@article{StoeckleinMakowerBieretal.1997,
  author    = {St{\"o}cklein, Walter F. M. and Makower, Alexander and Bier, Frank Fabian and Scheller, Frieder W.},
  title     = {Enzyme sensors and enzyme amplifification systems},
  year      = {1997},
  language  = {en}
}
@article{KatterleWollenbergerScheller1997,
  author    = {Katterle, Martin and Wollenberger, Ursula and Scheller, Frieder W.},
  title     = {Electrochemistry of hemoglobin at modified silver electrodes is not a redox-process of iron protoporhyrin IX},
  year      = {1997},
  language  = {en}
}
@article{SchulmeisterRoseScheller1997,
  author    = {Schulmeister, Thomas and Rose, J{\"u}rgen and Scheller, Frieder W.},
  title     = {Mathematical modelling of exponential amplification in membrane-based enzyme sensors},
  year      = {1997},
  language  = {en}
}
@article{MakowerBarminMorzunovaetal.1997,
  author    = {Makower, Alexander and Barmin, Anatoli V. and Morzunova, T. and Eremenko, Arkadi V. and Bier, Frank Fabian and Scheller, Frieder W.},
  title     = {Affinity enzymomoetric assay for detection of organophosphorus compounds},
  year      = {1997},
  language  = {en}
}
@article{SchellerPfeiffer1997,
  author    = {Scheller, Frieder W. and Pfeiffer, Dorothea},
  title     = {Commercial devices based on amperometric biosensors},
  year      = {1997},
  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{FreaneyMacShaneKeavenyetal.1997,
  author    = {Freaney, R. and MacShane, A. and Keaveny, T. V. and MacKenna, M. and Rabenstein, K. and Scheller, Frieder W. and Pfeiffer, Dorothea and Urban, G. and Moser, I. and Jobst, G. and Manz, A. and Verpoorte, E. and Widmer, M. W. and Diamond, D. and Dempsey, E. and deViteri, F. J. S. and Smyth, M.},
  title     = {Novel instrumentation for real-time monitoring using miniaturized flow systems with integrated biosensors},
  year      = {1997},
  language  = {en}
}
@article{SchellerPfeifferLisdatetal.1998,
  author    = {Scheller, Frieder W. and Pfeiffer, Dorothea and Lisdat, Fred and Bauer, Christian G. and Gajovic, Nenad},
  title     = {Enzyme biosensors based on oxygen detection},
  year      = {1998},
  language  = {en}
}
@article{SchellerKleinjungBieretal.1998,
  author    = {Scheller, Frieder W. and Kleinjung, Frank and Bier, Frank Fabian and Markower, Alexander and Neumann, Barbara and Wollenberger, Ursula and Kurochkin, Iliya N. and Eremenko, Arkadi V. and Barmin, Anatoli V. and Klußmann, Sven and F{\"u}rste, Jens-Peter and Erdmann, Volker A. and Mansuy, D.},
  title     = {New recognition elements in biosensing},
  year      = {1998},
  language  = {en}
}