@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{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{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{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{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{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{SigolaevaMarkowerEremenkoetal.2001, author = {Sigolaeva, L. V. and Markower, Alexander and Eremenko, A. V. and Makhaeva, G. F. and Malygin, V. V. and Kurochkin, I. N. and Scheller, Frieder W.}, title = {Bioelectrochemical anaysis of neuropathy targes esterase activity in blood}, year = {2001}, 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{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{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} } @misc{SchellerZhangYarmanetal.2019, author = {Scheller, Frieder W. and Zhang, Xiaorong and Yarman, Aysu and Wollenberger, Ulla and Gyurcs{\´a}nyi, R{\´o}bert E.}, title = {Molecularly imprinted polymer-based electrochemical sensors for biopolymers}, series = {Current opinion in electrochemistry}, volume = {14}, journal = {Current opinion in electrochemistry}, publisher = {Elsevier}, address = {Amsterdam}, issn = {2451-9103}, doi = {10.1016/j.coelec.2018.12.005}, pages = {53 -- 59}, year = {2019}, abstract = {Electrochemical synthesis and signal generation dominate among the almost 1200 articles published annually on protein-imprinted polymers. Such polymers can be easily prepared directly on the electrode surface, and the polymer thickness can be precisely adjusted to the size of the target to enable its free exchange. In this architecture, the molecularly imprinted polymer (MIP) layer represents only one 'separation plate'; thus, the selectivity does not reach the values of 'bulk' measurements. The binding of target proteins can be detected straightforwardly by their modulating effect on the diffusional permeability of a redox marker through the thin MIP films. However, this generates an 'overall apparent' signal, which may include nonspecific interactions in the polymer layer and at the electrode surface. Certain targets, such as enzymes or redox active proteins, enables a more specific direct quantification of their binding to MIPs by in situ determination of the enzyme activity or direct electron transfer, respectively.}, 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{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{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{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{SchellerWollenbergerLeietal.2002, author = {Scheller, Frieder W. and Wollenberger, Ursula and Lei, Chenghong and Jin, Wen and Ge, Bixia and Lehmann, Claudia and Lisdat, Fred and Fridman, Vadim}, title = {Bioelectrocatalysis by redox enzymes at modified electrodes}, year = {2002}, language = {en} } @article{SchellerWollenberger2003, author = {Scheller, Frieder W. and Wollenberger, Ursula}, title = {Enzyme Electrodes}, isbn = {3-527-30401-0}, year = {2003}, language = {en} } @article{SchellerWagener2004, author = {Scheller, Frieder W. and Wagener, C.}, title = {From gene to life}, year = {2004}, 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{SchellerSchmid2020, author = {Scheller, Frieder W. and Schmid, Rolf}, title = {A tribute to Isao Karube (1942-2020) and his influence on sensor science}, series = {Analytical and bioanalytical chemistry : a merger of Fresenius' journal of analytical chemistry, Analusis and Quimica analitica}, volume = {412}, journal = {Analytical and bioanalytical chemistry : a merger of Fresenius' journal of analytical chemistry, Analusis and Quimica analitica}, number = {28}, publisher = {Springer}, address = {Berlin}, issn = {1618-2642}, doi = {10.1007/s00216-020-02946-5}, pages = {7709 -- 7711}, year = {2020}, language = {en} }