@misc{TanneGoebelLisdat2011, author = {Tanne, Christoph K. and G{\"o}bel, Gero and Lisdat, Fred}, title = {Entwicklung einer Glucosedehydrogenase-basierten Anode und deren Anwendung in einer Glucose/O2-Biobrennstoffzelle}, series = {Wissenschaftliche Beitr{\"a}ge 2011}, volume = {15}, journal = {Wissenschaftliche Beitr{\"a}ge 2011}, issn = {0949-8214}, doi = {10.15771/0949-8214_2011_1_2}, url = {http://nbn-resolving.de/urn:nbn:de:kobv:526-opus-1039}, pages = {13 -- 21}, year = {2011}, abstract = {Unter Verwendung von mehrwandigen Kohlenstoffnanor{\"o}hren wurde in dieser Studie eine neuartige Anode zum Einsatz in Biobrennstoffzellen entwickelt. Dazu wurde das rekombinante Enzym Pyrrolochinolinchinon(PQQ)- abh{\"a}ngige Glucosedehydrogenase kovalent an eine aus PQQ bestehenden Zwischenschicht gekoppelt, welche zuvor an die Kohlenstoffnanor{\"o}hren adsorbiert war. Die Nanor{\"o}hren wurden aufgrund ihrer Thiolmodifikation chemisorptiv auf einer Goldelektrode gebunden. In glucosehaltiger L{\"o}sung konnte der Start eines katalytischen Stroms bei einem Potential von -80 mV vs. Ag/AgCl (1 MKCl) beobachtet werden. Unter Substrats{\"a}ttigung wurden Stromdichten im Bereich von 170 bis 200 μA/cm2 gemessen. Dieses System basiert auf einem mediatorvermittelten Elektronentransfer. Die entwickelte (PQQ)-GDH-MWCNT-Elektrode wurde mit einer MWCNT-modifizierten Elektrode kombiniert, bei der Bilirubinoxidase (BOD) als Biokatalysator fungiert. Daraus resultierte eine membranfreie Biobrennstoffzelle mit einem leichgewichtspotential von 600 mV und Leistungsdichten im Bereich von 20-25 μW/cm2.}, language = {de} } @misc{SchubartGoebelLisdat2013, author = {Schubart, Ivo and G{\"o}bel, Gero and Lisdat, Fred}, title = {Direkte Kontaktierung des Enzyms (PQQ)-GDH und Elektroden mit Hilfe von polymermodifizierten Nanor{\"o}hren f{\"u}r die Anwendung in Biobrennstoffzellen}, series = {Wissenschaftliche Beitr{\"a}ge 2013}, volume = {17}, journal = {Wissenschaftliche Beitr{\"a}ge 2013}, issn = {0949-8214}, doi = {10.15771/0949-8214_2013_1_3}, url = {http://nbn-resolving.de/urn:nbn:de:kobv:526-opus4-3127}, pages = {17 -- 22}, year = {2013}, abstract = {In dieser Studie pr{\"a}sentieren wir eine Enzymelektrode, bei der ein direkter Elektronentransfer (DET) zwischen der Pyrrolochinolinchinon-abh{\"a}ngigen Glukosedehydrogenase (PQQ)-GDH und einer Elektrode realisiert werden konnte. Hierf{\"u}r wird eine Goldelektrode mit mehrwandigen Kohlenstoffnanor{\"o}hren [engl. multi-walled carbon nanotubes (MWCNT)] modifiziert, anschließend mit einem Copolymer aus Anilinderivaten {\"u}berzogen und dann die (PQQ)-GDH (Acinetobacter calcoaceticus) kovalent immobilisiert. Die gepulste Polymersynthese wird hinsichtlich der Effektivit{\"a}t der bioelektrokatalytischen Umsetzung von Glukose optimiert. Die Glukoseoxidation startet bei einem Potential von -0,1 V vs. Ag/AgCl (1 M KCl) und Stromdichten von bis zu 500 μA/cm² (+0,1 V) k{\"o}nnen erreicht werden. Der Messbereich f{\"u}r Glukose liegt bei 0,1-5 mM (+0,1 V vs. Ag/AgCl). Der dynamische Bereich ist bei h{\"o}herem Potential auf bis zu 100 mM (+0,4 V vs Ag/AgCl) erweitert. Die Elektrode wird als Anode in einer Biobrennstoffzelle (BBZ) mit einer Bilirubinoxidase-modifizierten MWCNT/Gold-Kathode eingesetzt. Beide Elektroden basieren auf einem DET. Das Zellpotential der BBZ betr{\"a}gt 680 ±20 mV und sie erreicht eine maximale Leistungsdichte von 65 μW/cm² (bei einer Zellspannung von 350 mV).}, language = {de} } @article{KhalidGoebelHuehnetal.2011, author = {Khalid, Waqas and G{\"o}bel, Gero and H{\"u}hn, Dominik and Montenegro, Jose-Maria and Rivera-Gil, Pilar and Lisdat, Fred and Parak, Wolfgang J.}, title = {Light triggered detection of aminophenyl phosphate with a quantum dot based enzyme electrode}, series = {Journal of Nanobiotechnology}, volume = {9}, journal = {Journal of Nanobiotechnology}, number = {46}, issn = {1477-3155}, url = {http://nbn-resolving.de/urn:nbn:de:kobv:526-opus4-5808}, pages = {10}, year = {2011}, abstract = {An electrochemical sensor for p-aminophenyl phosphate (p APP) is reported. It is based on the electrochemical conversion of 4-aminophenol (4AP) at a quantum dot (QD) modified electrode under illumination. Without illumination no electron transfer and thus no oxidation of 4AP can occur. p APP as substrate is converted by the enzyme alkaline phosphatase (ALP) to generate 4AP as a product. The QDs are coupled via 1,4-benzenedithiol (BDT) linkage to the surface of a gold electrode and thus allow potential-controlled photocurrent generation. The photocurrent is modified by the enzyme reaction providing access to the substrate detection. In order to develop a photobioelectrochemical sensor the enzyme is immobilized on top of the photo-switchable layer of the QDs. Immobilization of ALP is required for the potential possibility of spatially resolved measurements. Geometries with immobilized ALP are compared versus having the ALP in solution. Data indicate that functional immobilization with layer-by-layer assembly is possible. Enzymatic activity of ALP and thus the photocurrent can be described by Michaelis- Menten kinetics. p APP is detected as proof of principle investigation within the range of 25 μM - 1 mM.}, language = {en} } @article{GoebelTalkeAhnertetal.2019, author = {G{\"o}bel, Gero and Talke, Anja and Ahnert, Uwe and Lisdat, Fred}, title = {Electrochemical Activity Determination of Catechol-O-methyl Transferase by Selective Dopamine Detection}, series = {ChemElectroChem}, volume = {6}, journal = {ChemElectroChem}, number = {17}, publisher = {Wiley}, doi = {10.1002/celc.201900856}, url = {http://nbn-resolving.de/urn:nbn:de:kobv:526-opus4-13900}, pages = {4533 -- 4540}, year = {2019}, abstract = {Abstract For the treatment of Parkinson's disease, as one of the most frequent diseases of the central nervous system, several key enzymes for dopamine metabolism [e. g. catechol-O-methyl transferase (COMT)] are drug targets. For an efficient and long-lasting treatment, the activity of this enzyme should be monitored. In this study, an electrochemical approach using differential pulse voltammetry (DPV) is introduced for the activity determination. The applied electrode material, fluorine-doped tin oxide (FTO), is characterized by a clear discrimination between substrate and product of COMT, a high stability of the dopamine signal during consecutive measurements, and a linear dependency on the dopamine concentration in the range of the maximum reaction rate of COMT. Despite these advantageous results, dopamine detection in the complete activity assay is influenced by each of the added essential assay components, even though none of the added components reveal a current signal at the FTO electrode itself. After adjusting the potential range and the assay composition, these effects can be circumvented. By following the dopamine concentrations during COMT action, it can be shown that the activity of COMT can be detected by using differential pulse voltammetry (DPV) at an FTO electrode and, by analyzing different COMT amounts, quantification can be demonstrated.}, language = {en} } @article{GoebelDietzLisdat2009, author = {G{\"o}bel, Gero and Dietz, T. and Lisdat, Fred}, title = {Biosensor based on an oxygen reducing bilirubin oxidase electrode}, series = {Procedia Chemistry}, volume = {1}, journal = {Procedia Chemistry}, number = {1}, issn = {1876-6196}, doi = {10.1016/j.proche.2009.07.068}, url = {http://nbn-resolving.de/urn:nbn:de:kobv:526-opus4-6237}, pages = {273 -- 276}, year = {2009}, abstract = {An oxygen reducing electrode made of bilirubin oxidase and multi-walled carbon nanotubes (BOD-MWCNT-Au electrode) is coupled to enzymes catalysing oxygen-consuming reactions such as glucose oxidase (GOD) to result in a membrane-free bienzyme electrode. The feasibility of such a molecularly assembled system stabilized by covalent linkage has been demonstrated. The electrochemical characterisation of the bienzyme electrode reveals sensitivity to the enzyme substrate. The results indicate that the BOD-electrode provides a suitable platform for sensing analytes for which oxidases of high activity are available.}, language = {en} } @inproceedings{RiedelGoebelParaketal.2014, author = {Riedel, Marc and G{\"o}bel, Gero and Parak, Wolfgang J. and Lisdat, Fred}, title = {Light-addressable amperometric electrodes for enzyme sensors based on direct quantum dot-electrode contacts}, publisher = {Society of Photo-Optical Instrumentation Engineers (SPIE)}, url = {http://nbn-resolving.de/urn:nbn:de:kobv:526-opus4-15266}, pages = {195 -- 200}, year = {2014}, abstract = {Quantum dots allow the generation of charge carriers upon illumination. When these particles are attached to an electrode a photocurrent can be generated. This allows their use as a light-switchable layer on the surface. The QDs can not only exchange electronics with the electrode, but can also interact with donor or acceptor compounds in solution providing access to the construction of signal chains starting from an analytic molecule. The magnitude and the direction of the photocurrent depend on several factors such as electrode polarization, solution pH and composition. These defined dependencies have been evaluated with respect to the combination of QD-electrodes with enzyme reactions for sensorial purpose. CdSe/ZnS-QD-modified electrodes can be used to follow enzymatic reactions in solution based on the oxygen sensitivity. In order to develop a photoelectrochemical biosensor, e.g. glucose oxidase is immobilized on the CdSe/ZnS-electrode. One immobilization strategy applies the layer-by-layer-technique of GOD and a polyelectrolyte. Photocurrent measurements of such a sensor show a clear concentration dependent behavior. The principle of combing QD oxidase. The sensitivity of quantum dot electrodes can be influenced by additional nanoparticles, but also by multiple layers of the QDs. In another direction of research it can be influenced by additional nanoparticles, but also by multiple layers of the QDs. In another direction of research it can be demonstrated that direct electron transfer from excited quantum dots can be achieved with the redox protein cytochrome c. This allows the detection of the protein, but also interaction partners such as a enzymes or superoxide.}, language = {en} }