TY - JOUR A1 - Shumyantseva, V. V. A1 - Ivanov, Y. D. A1 - Bistolas, Nikitas A1 - Scheller, Frieder W. A1 - Archakov, Alexander I. A1 - Wollenberger, Ursula T1 - Direct electron transfer of cytochrome P450 2B4 at electrodes modified with non-ionic detergent and colloidal clay nanoparticles N2 - 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 Y1 - 2004 ER - TY - JOUR A1 - Sezer, Murat A1 - Spricigo, Roberto A1 - Utesch, Tillmann A1 - Millo, Diego A1 - Leimkühler, Silke A1 - Mroginski, Maria A. A1 - Wollenberger, Ursula A1 - Hildebrandt, Peter A1 - Weidinger, Inez M. T1 - Redox properties and catalytic activity of surface-bound human sulfite oxidase studied by a combined surface enhanced resonance Raman spectroscopic and electrochemical approach N2 - Human sulfite oxidase (hSO) was immobilised on SAM-coated silver electrodes under preservation of the native heme pocket structure of the cytochrome b5 (Cyt b5) domain and the functionality of the enzyme. The redox properties and catalytic activity of the entire enzyme were studied by surface enhanced resonance Raman (SERR) spectroscopy and cyclic voltammetry (CV) and compared to the isolated heme domain when possible. It is shown that heterogeneous electron transfer and catalytic activity of hSO sensitively depend on the local environment of the enzyme. Increasing the ionic strength of the buffer solution leads to an increase of the heterogeneous electron transfer rate from 17 s(-1) to 440 s(- 1) for hSO as determined by SERR spectroscopy. CV measurements demonstrate an increase of the apparent turnover rate for the immobilised hSO from 0.85 s(-1) in 100 mM buffer to 5.26 s(-1) in 750 mM buffer. We suggest that both effects originate from the increased mobility of the surface-bound enzyme with increasing ionic strength. In agreement with surface potential calculations we propose that at high ionic strength the enzyme is immobilised via the dimerisation domain to the SAM surface. The flexible loop region connecting the Moco and the Cyt b5 domain allows alternating contact with the Moco interaction site and the SAM surface, thereby promoting the sequential intramolecular and heterogeneous electron transfer from Moco via Cyt b5 to the electrode. At lower ionic strength, the contact time of the Cyt b5 domain with the SAM surface is longer, corresponding to a slower overall electron transfer process. Y1 - 2010 UR - http://www.rsc.org/Publishing/Journals/CP/index.asp U6 - https://doi.org/10.1039/B927226g SN - 1463-9076 ER - TY - JOUR A1 - Scheller, Frieder W. A1 - Yarman, Aysu A1 - Bachmann, Till A1 - Hirsch, Thomas A1 - Kubick, Stefan A1 - Renneberg, Reinhard A1 - Schumacher, Soeren A1 - Wollenberger, Ursula A1 - Teller, Carsten A1 - Bier, Frank Fabian ED - Gu, MB ED - Kim, HS T1 - Future of biosensors: a personal view JF - Advances in biochemical engineering, biotechnology JF - Advances in Biochemical Engineering-Biotechnology N2 - 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. KW - Biosensors KW - Molecularly imprinted polymers KW - Personalized medicine Y1 - 2014 SN - 978-3-642-54143-8; 978-3-642-54142-1 U6 - https://doi.org/10.1007/10_2013_251 SN - 0724-6145 VL - 140 SP - 1 EP - 28 PB - Springer CY - Berlin ER - TY - JOUR A1 - Scheller, Frieder W. A1 - Wollenberger, Ursula A1 - Warsinke, Axel A1 - Lisdat, Fred T1 - Research and development in biosensors Y1 - 2001 ER - TY - JOUR A1 - Scheller, Frieder W. A1 - Wollenberger, Ursula A1 - Schubert, Florian A1 - Pfeiffer, Dorothea A1 - Markower, Alexander A1 - McNeil, C. J. T1 - Multienzyme biosensors : coupled enzyme reactions and enzyme activation Y1 - 1993 ER - TY - JOUR A1 - Scheller, Frieder W. A1 - Wollenberger, Ursula A1 - Pfeiffer, Dorothea A1 - Schubert, Florian T1 - Overview of biosensor technology : proceedings of Mosbach Symposion on Biochemical Technology Y1 - 1996 ER - TY - JOUR A1 - Scheller, Frieder W. A1 - Wollenberger, Ursula A1 - Lei, Chenghong A1 - Jin, Wen A1 - Ge, Bixia A1 - Lehmann, Claudia A1 - Lisdat, Fred A1 - Fridman, Vadim T1 - Bioelectrocatalysis by redox enzymes at modified electrodes Y1 - 2002 UR - www.elsevier.nl/inca/publications/6/0/1/3/4/7/index.htt ER - TY - JOUR A1 - Scheller, Frieder W. A1 - Wollenberger, Ursula T1 - Enzyme Electrodes Y1 - 2003 SN - 3-527-30401-0 ER - TY - JOUR A1 - Scheller, Frieder W. A1 - Pfeiffer, Dorothea A1 - Schubert, Florian A1 - Wollenberger, Ursula T1 - Enzyme - based electrodes Y1 - 1995 ER - TY - JOUR A1 - Scheller, Frieder W. A1 - Makower, Alexander A1 - Ghindilis, A. L. A1 - Bier, Frank Fabian A1 - Ehrentreich-Förster, Eva A1 - Wollenberger, Ursula A1 - Bauer, Christian G. A1 - Micheel, Burkhard A1 - Pfeiffer, Dorothea A1 - Szeponik, Jan A1 - Michael, N. A1 - Kaden, H. T1 - Enzyme sensors for subnanomolar concentrations Y1 - 1995 ER - TY - JOUR A1 - Scheller, Frieder W. A1 - Makower, Alexander A1 - Bier, Frank Fabian A1 - Wollenberger, Ursula A1 - Ghindilis, A. L. A1 - Eremenko, A. V. A1 - Pfeiffer, Dorothea T1 - Enzymsensoren zur Bestimmung subnanomolarer Konzentrationen Y1 - 1995 ER - TY - JOUR A1 - Scheller, Frieder W. A1 - Lisdat, Fred A1 - Wollenberger, Ursula T1 - Application of electrically contacted enzymes for biosensors Y1 - 2005 SN - 3-527- 30690-0 ER - TY - JOUR A1 - Scheller, Frieder W. A1 - Kleinjung, Frank A1 - Bier, Frank Fabian A1 - Markower, Alexander A1 - Neumann, Barbara A1 - Wollenberger, Ursula A1 - Kurochkin, Iliya N. A1 - Eremenko, Arkadi V. A1 - Barmin, Anatoli V. A1 - Klußmann, Sven A1 - Fürste, Jens-Peter A1 - Erdmann, Volker A. A1 - Mansuy, D. T1 - New recognition elements in biosensing Y1 - 1998 ER - TY - JOUR A1 - Scheller, Frieder W. A1 - Jin, Wen A1 - Ehrentreich-Förster, Eva A1 - Ge, Bixia A1 - Lisdat, Fred A1 - Büttemeyer, R. A1 - Wollenberger, Ursula T1 - Cytochrome c based superoxide sensor for in vivo application Y1 - 1999 ER - TY - JOUR A1 - Scheller, Frieder W. A1 - Bistolas, Nikitas A1 - Liu, Songqin A1 - Jänchen, Michael A1 - Katterle, Martin A1 - Wollenberger, Ursula T1 - Thirty years of haemoglobin electrochemistry N2 - 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 Y1 - 2005 ER - TY - JOUR A1 - Scheller, Frieder W. A1 - Bauer, Christian G. A1 - Markower, Alexander A1 - Wollenberger, Ursula A1 - Warsinke, Axel A1 - Bier, Frank Fabian T1 - Coupling of immunoassays with enzymatic recycling electrodes Y1 - 2001 ER - TY - JOUR A1 - Scheller, Frieder W. A1 - Bauer, Christian G. A1 - Makower, Alexander A1 - Wollenberger, Ursula A1 - Warsinke, Axel A1 - Bier, Frank Fabian T1 - Immunoassays using enzymatic amplification electrodes Y1 - 2002 SN - 0-7484-0791-X ER - TY - JOUR A1 - Sarauli, David A1 - Riedel, Marc A1 - Wettstein, Christoph A1 - Hahn, Robert A1 - Stiba, Konstanze A1 - Wollenberger, Ursula A1 - Leimkühler, Silke A1 - Schmuki, Patrik A1 - Lisdat, Fred T1 - Semimetallic TiO2 nanotubes new interfaces for bioelectrochemical enzymatic catalysis JF - Journal of materials chemistry N2 - Different self-organized TiO2 nanotube structures are shown to represent new interfaces for the achievement of bioelectrochemical enzymatic catalysis involving redox proteins and enzymes without further surface modification or the presence of mediators. Y1 - 2012 U6 - https://doi.org/10.1039/c2jm16427b SN - 0959-9428 VL - 22 IS - 11 SP - 4615 EP - 4618 PB - Royal Society of Chemistry CY - Cambridge ER - TY - JOUR A1 - Rose, Andreas A1 - Pfeiffer, Dorothea A1 - Scheller, Frieder W. A1 - Wollenberger, Ursula T1 - Quinoprotein glucose dehydrogenasemodified thick-film electrodes for the amperometric detection of phenolic compounds in flow injection analysis Y1 - 2001 ER - TY - JOUR A1 - Pinyou, Piyanut A1 - Ruff, Adrian A1 - Poeller, Sascha A1 - Alsaoub, Sabine A1 - Leimkühler, Silke A1 - Wollenberger, Ursula A1 - Schuhmann, Wolfgang T1 - Wiring of the aldehyde oxidoreductase PaoABC to electrode surfaces via entrapment in low potential phenothiazine-modified redox polymers JF - Bioelectrochemistry : an international journal devoted to electrochemical aspects of biology and biological aspects of electrochemistry ; official journal of the Bioelectrochemical Society N2 - Phenothiazine-modified redox hydrogels were synthesized and used for the wiring of the aldehyde oxidoreductase PaoABC to electrode surfaces. The effects of the pH value and electrode surface modification on the biocatalytic activity of the layers were studied in the presence of vanillin as the substrate. The enzyme electrodes were successfully employed as bioanodes in vanillin/O-2 biofuel cells in combination with a high potential bilirubin oxidase biocathode. Open circuit voltages of around 700 mV could be obtained in a two compartment biofuel cell setup. Moreover, the use of a rather hydrophobic polymer with a high degree of crosslinking sites ensures the formation of stable polymer/enzyme films which were successfully used as bioanode in membrane-less biofuel cells. (C) 2015 Elsevier B.V. All rights reserved. KW - Aldehyde oxidoreductase KW - Enzyme electrode KW - Redox polymer KW - Phenothiazine KW - Biosensor KW - Biofuel cell Y1 - 2016 U6 - https://doi.org/10.1016/j.bioelechem.2015.12.005 SN - 1567-5394 SN - 1878-562X VL - 109 SP - 24 EP - 30 PB - Elsevier CY - Lausanne ER -