TY - JOUR A1 - Welzel, H.-P. A1 - Kossmehl, G. A1 - Engelmann, G. A1 - Neumann, B. A1 - Wollenberger, Ursula A1 - Scheller, Frieder W. A1 - Schröder, W. T1 - Reactive groups on polymer covered electrodes, 4. Lactate-oxidase-biosensor based on electrodes modifies by polyphiophene Y1 - 1996 ER - TY - JOUR A1 - Neumann, Bettina A1 - Götz, Robert A1 - Wrzolek, Pierre A1 - Scheller, Frieder W. A1 - Weidinger, Inez M. A1 - Schwalbe, Matthias A1 - Wollenberger, Ulla T1 - Enhancement of the Electrocatalytic Activity of Thienyl-Substituted Iron Porphyrin Electropolymers by a Hangman Effect JF - ChemCatChem : heterogeneous & homogeneous & bio- & nano-catalysis ; a journal of ChemPubSoc Europe N2 - The thiophene-modified iron porphyrin FeT3ThP and the respective iron Hangman porphyrin FeH3ThP, incorporating a carboxylic acid hanging group in the second coordination sphere of the iron center, were electropolymerized on glassy carbon electrodes using 3,4-ethylenedioxythiophene (EDOT) as co-monomer. Scanning electron microscopy images and Resonance Raman spectra demonstrated incorporation of the porphyrin monomers into a fibrous polymer network. Porphyrin/polyEDOT films catalyzed the reduction of molecular oxygen in a four-electron reaction to water with onset potentials as high as +0.14V vs. Ag/AgCl in an aqueous solution of pH7. Further, FeT3ThP/polyEDOT films showed electrocatalytic activity towards reduction of hydrogen peroxide at highly positive potentials, which was significantly enhanced by introduction of the carboxylic acid hanging group in FeH3ThP. The second coordination sphere residue promotes formation of a highly oxidizing reaction intermediate, presumably via advantageous proton supply, as observed for peroxidases and catalases making FeH3ThP/polyEDOT films efficient mimics of heme enzymes. KW - activation of oxygen species KW - electro-polymerization KW - Hangman porphyrin KW - heterogeneous catalysis KW - immobilization Y1 - 2018 U6 - https://doi.org/10.1002/cctc.201800934 SN - 1867-3880 SN - 1867-3899 VL - 10 IS - 19 SP - 4353 EP - 4361 PB - Wiley-VCH CY - Weinheim ER - TY - GEN A1 - Yarman, Aysu A1 - Jetzschmann, Katharina J. A1 - Neumann, Bettina A1 - Zhang, Xiaorong A1 - Wollenberger, Ulla A1 - Cordin, Aude A1 - Haupt, Karsten A1 - Scheller, Frieder W. T1 - Enzymes as tools in MIP-sensors T2 - Postprints der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe N2 - Molecularly imprinted polymers (MIPs) have the potential to complement antibodies in bioanalysis, are more stable under harsh conditions, and are potentially cheaper to produce. However, the affinity and especially the selectivity of MIPs are in general lower than those of their biological pendants. Enzymes are useful tools for the preparation of MIPs for both low and high-molecular weight targets: As a green alternative to the well-established methods of chemical polymerization, enzyme-initiated polymerization has been introduced and the removal of protein templates by proteases has been successfully applied. Furthermore, MIPs have been coupled with enzymes in order to enhance the analytical performance of biomimetic sensors: Enzymes have been used in MIP-sensors as tracers for the generation and amplification of the measuring signal. In addition, enzymatic pretreatment of an analyte can extend the analyte spectrum and eliminate interferences. T3 - Zweitveröffentlichungen der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe - 1098 KW - enzymatic MIP synthesis KW - template digestion KW - enzyme tracer KW - enzymatic analyte conversion KW - molecularly imprinted polymers Y1 - 2021 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:517-opus4-474642 SN - 1866-8372 IS - 1098 ER - TY - JOUR A1 - Yarman, Aysu A1 - Jetzschmann, Katharina J. A1 - Neumann, Bettina A1 - Zhang, Xiaorong A1 - Wollenberger, Ulla A1 - Cordin, Aude A1 - Haupt, Karsten A1 - Scheller, Frieder W. T1 - Enzymes as Tools in MIP-Sensors JF - Chemosensors N2 - Molecularly imprinted polymers (MIPs) have the potential to complement antibodies in bioanalysis, are more stable under harsh conditions, and are potentially cheaper to produce. However, the affinity and especially the selectivity of MIPs are in general lower than those of their biological pendants. Enzymes are useful tools for the preparation of MIPs for both low and high-molecular weight targets: As a green alternative to the well-established methods of chemical polymerization, enzyme-initiated polymerization has been introduced and the removal of protein templates by proteases has been successfully applied. Furthermore, MIPs have been coupled with enzymes in order to enhance the analytical performance of biomimetic sensors: Enzymes have been used in MIP-sensors as tracers for the generation and amplification of the measuring signal. In addition, enzymatic pretreatment of an analyte can extend the analyte spectrum and eliminate interferences. KW - enzymatic MIP synthesis KW - template digestion KW - enzyme tracer KW - enzymatic analyte conversion KW - molecularly imprinted polymers Y1 - 2017 U6 - https://doi.org/10.3390/chemosensors5020011 SN - 2227-9040 VL - 5 PB - MDPI CY - Basel ER - TY - JOUR A1 - Scheller, Frieder W. A1 - Bier, Frank Fabian A1 - Neumann, B. T1 - Bioindikation in aquatischen Ökosystemen : Bioindikation in limnischen und küstennahen Ökosystemen ; Grundlagen, Verfahren und Methoden Y1 - 1994 PB - Fischer CY - Jena ER - TY - JOUR A1 - Grott, Matthias A1 - Knollenberg, J. A1 - Hamm, M. A1 - Ogawa, K. A1 - Jaumann, R. A1 - Otto, Katharina Alexandra A1 - Delbo, M. A1 - Michel, P. A1 - Biele, J. A1 - Neumann, W. A1 - Knapmeyer, M. A1 - Kuehrt, E. A1 - Senshu, H. A1 - Okada, T. A1 - Helbert, J. A1 - Maturilli, A. A1 - Müller, N. A1 - Hagermann, A. A1 - Sakatani, N. A1 - Tanaka, S. A1 - Arai, T. A1 - Mottola, S. A1 - Tachibana, S. A1 - Pelivan, Ivanka A1 - Drube, L. A1 - Vincent, J-B A1 - Yano, H. A1 - Pilorget, C. A1 - Matz, K. D. A1 - Schmitz, N. A1 - Koncz, A. A1 - Schröder, S. E. A1 - Trauthan, F. A1 - Schlotterer, M. A1 - Krause, C. A1 - Ho, T-M A1 - Moussi-Soffys, A. T1 - Low thermal conductivity boulder with high porosity identified on C-type asteroid (162173) Ryugu JF - Nature astronomy N2 - C-type asteroids are among the most pristine objects in the Solar System, but little is known about their interior structure and surface properties. Telescopic thermal infrared observations have so far been interpreted in terms of a regolith-covered surface with low thermal conductivity and particle sizes in the centimetre range. This includes observations of C-type asteroid (162173) Ryugu1,2,3. However, on arrival of the Hayabusa2 spacecraft at Ryugu, a regolith cover of sand- to pebble-sized particles was found to be absent4,5 (R.J. et al., manuscript in preparation). Rather, the surface is largely covered by cobbles and boulders, seemingly incompatible with the remote-sensing infrared observations. Here we report on in situ thermal infrared observations of a boulder on the C-type asteroid Ryugu. We found that the boulder’s thermal inertia was much lower than anticipated based on laboratory measurements of meteorites, and that a surface covered by such low-conductivity boulders would be consistent with remote-sensing observations. Our results furthermore indicate high boulder porosities as well as a low tensile strength in the few hundred kilopascal range. The predicted low tensile strength confirms the suspected observational bias6 in our meteorite collections, as such asteroidal material would be too frail to survive atmospheric entry7. Y1 - 2020 U6 - https://doi.org/10.1038/s41550-019-0832-x SN - 2397-3366 VL - 3 IS - 11 SP - 971 EP - 976 PB - Nature Publishing Group CY - London ER - TY - JOUR A1 - Welzel, H.-P. A1 - Kossmehl, G. A1 - Engelmann, G. A1 - Neumann, B. A1 - Wollenberger, Ursula A1 - Scheller, Frieder W. T1 - Electrochemical polymerization of functionalized thiohene derivatives for immobilization of proteins Y1 - 1997 ER - TY - JOUR A1 - Li, Junbai A1 - Miller, Reinhard A1 - Wüstneck, Rainer A1 - Möhwald, Helmuth A1 - Neumann, A. W. T1 - News of pendant drop technique as a film balance at liquid/liquid interfaces Y1 - 1995 ER - TY - JOUR A1 - Riedel, K. A1 - Beyersdorf-Radeck, Baerbel A1 - Neumann, B. A1 - Scheller, Frieder W. A1 - Schmid, Rolf D. T1 - Microbial sensors for determination of aromatics and their chloro derivatives. Part III: Determination of chlorinated phenols using a biosensor containing Trichosporon beigelii (cutaneum) Y1 - 1995 ER - TY - JOUR A1 - Wollenberger, Ursula A1 - Neumann, B. A1 - Scheller, Frieder W. T1 - Development of a biomimetic alkane sensor f Y1 - 1998 ER - TY - JOUR A1 - Wollenberger, Ursula A1 - Neumann, B. A1 - Riedel, K. A1 - Scheller, Frieder W. T1 - Enzyme and microbial sensors for phosphate, phenols, pesticides and peroxides Y1 - 1994 ER - TY - JOUR A1 - Bruma, Maria A1 - Mercer, Frank W. A1 - Schulz, Burkhard A1 - Dietel, Reinhard A1 - Neumann, Werner T1 - Fluorinated poly(benzoxazole-imide)s Y1 - 1994 ER - TY - JOUR A1 - Wollenberger, Ursula A1 - Neumann, B. A1 - Scheller, Frieder W. T1 - Enzyme and microbial sensors for environmental Monitoring Y1 - 1993 ER - TY - JOUR A1 - Chipman, Ariel D. A1 - Ferrier, David E. K. A1 - Brena, Carlo A1 - Qu, Jiaxin A1 - Hughes, Daniel S. T. A1 - Schroeder, Reinhard A1 - Torres-Oliva, Montserrat A1 - Znassi, Nadia A1 - Jiang, Huaiyang A1 - Almeida, Francisca C. A1 - Alonso, Claudio R. A1 - Apostolou, Zivkos A1 - Aqrawi, Peshtewani A1 - Arthur, Wallace A1 - Barna, Jennifer C. J. A1 - Blankenburg, Kerstin P. A1 - Brites, Daniela A1 - Capella-Gutierrez, Salvador A1 - Coyle, Marcus A1 - Dearden, Peter K. A1 - Du Pasquier, Louis A1 - Duncan, Elizabeth J. A1 - Ebert, Dieter A1 - Eibner, Cornelius A1 - Erikson, Galina A1 - Evans, Peter D. A1 - Extavour, Cassandra G. A1 - Francisco, Liezl A1 - Gabaldon, Toni A1 - Gillis, William J. A1 - Goodwin-Horn, Elizabeth A. A1 - Green, Jack E. A1 - Griffiths-Jones, Sam A1 - Grimmelikhuijzen, Cornelis J. P. A1 - Gubbala, Sai A1 - Guigo, Roderic A1 - Han, Yi A1 - Hauser, Frank A1 - Havlak, Paul A1 - Hayden, Luke A1 - Helbing, Sophie A1 - Holder, Michael A1 - Hui, Jerome H. L. A1 - Hunn, Julia P. A1 - Hunnekuhl, Vera S. A1 - Jackson, LaRonda A1 - Javaid, Mehwish A1 - Jhangiani, Shalini N. A1 - Jiggins, Francis M. A1 - Jones, Tamsin E. A1 - Kaiser, Tobias S. A1 - Kalra, Divya A1 - Kenny, Nathan J. A1 - Korchina, Viktoriya A1 - Kovar, Christie L. A1 - Kraus, F. Bernhard A1 - Lapraz, Francois A1 - Lee, Sandra L. A1 - Lv, Jie A1 - Mandapat, Christigale A1 - Manning, Gerard A1 - Mariotti, Marco A1 - Mata, Robert A1 - Mathew, Tittu A1 - Neumann, Tobias A1 - Newsham, Irene A1 - Ngo, Dinh N. A1 - Ninova, Maria A1 - Okwuonu, Geoffrey A1 - Ongeri, Fiona A1 - Palmer, William J. A1 - Patil, Shobha A1 - Patraquim, Pedro A1 - Pham, Christopher A1 - Pu, Ling-Ling A1 - Putman, Nicholas H. A1 - Rabouille, Catherine A1 - Ramos, Olivia Mendivil A1 - Rhodes, Adelaide C. A1 - Robertson, Helen E. A1 - Robertson, Hugh M. A1 - Ronshaugen, Matthew A1 - Rozas, Julio A1 - Saada, Nehad A1 - Sanchez-Gracia, Alejandro A1 - Scherer, Steven E. A1 - Schurko, Andrew M. A1 - Siggens, Kenneth W. A1 - Simmons, DeNard A1 - Stief, Anna A1 - Stolle, Eckart A1 - Telford, Maximilian J. A1 - Tessmar-Raible, Kristin A1 - Thornton, Rebecca A1 - van der Zee, Maurijn A1 - von Haeseler, Arndt A1 - Williams, James M. A1 - Willis, Judith H. A1 - Wu, Yuanqing A1 - Zou, Xiaoyan A1 - Lawson, Daniel A1 - Muzny, Donna M. A1 - Worley, Kim C. A1 - Gibbs, Richard A. A1 - Akam, Michael A1 - Richards, Stephen T1 - The first myriapod genome sequence reveals conservative arthropod gene content and genome organisation in the centipede Strigamia maritima JF - PLoS biology N2 - Myriapods (e. g., centipedes and millipedes) display a simple homonomous body plan relative to other arthropods. All members of the class are terrestrial, but they attained terrestriality independently of insects. Myriapoda is the only arthropod class not represented by a sequenced genome. We present an analysis of the genome of the centipede Strigamia maritima. It retains a compact genome that has undergone less gene loss and shuffling than previously sequenced arthropods, and many orthologues of genes conserved from the bilaterian ancestor that have been lost in insects. Our analysis locates many genes in conserved macro-synteny contexts, and many small-scale examples of gene clustering. We describe several examples where S. maritima shows different solutions from insects to similar problems. The insect olfactory receptor gene family is absent from S. maritima, and olfaction in air is likely effected by expansion of other receptor gene families. For some genes S. maritima has evolved paralogues to generate coding sequence diversity, where insects use alternate splicing. This is most striking for the Dscam gene, which in Drosophila generates more than 100,000 alternate splice forms, but in S. maritima is encoded by over 100 paralogues. We see an intriguing linkage between the absence of any known photosensory proteins in a blind organism and the additional absence of canonical circadian clock genes. The phylogenetic position of myriapods allows us to identify where in arthropod phylogeny several particular molecular mechanisms and traits emerged. For example, we conclude that juvenile hormone signalling evolved with the emergence of the exoskeleton in the arthropods and that RR-1 containing cuticle proteins evolved in the lineage leading to Mandibulata. We also identify when various gene expansions and losses occurred. The genome of S. maritima offers us a unique glimpse into the ancestral arthropod genome, while also displaying many adaptations to its specific life history. Y1 - 2014 U6 - https://doi.org/10.1371/journal.pbio.1002005 SN - 1545-7885 VL - 12 IS - 11 PB - PLoS CY - San Fransisco ER - TY - JOUR A1 - Neumann, Bettina A1 - Yarman, Aysu A1 - Wollenberger, Ursula A1 - Scheller, Frieder W. T1 - Characterization of the enhanced peroxidatic activity of amyloid beta peptide-hemin complexes towards neurotransmitters JF - Analytical & bioanalytical chemistry N2 - 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. KW - Peroxidatic activity Y1 - 2014 U6 - https://doi.org/10.1007/s00216-014-7822-8 SN - 1618-2642 SN - 1618-2650 VL - 406 IS - 14 SP - 3359 EP - 3364 PB - Springer CY - Heidelberg ER - TY - JOUR A1 - Yarman, Aysu A1 - Gröbe, Glenn A1 - Neumann, Bettina A1 - Kinne, Mathias A1 - Gajovic-Eichelmann, Nenad A1 - Wollenberger, Ursula A1 - Hofrichter, Martin A1 - Ullrich, Rene A1 - Scheibner, Katrin A1 - Scheller, Frieder W. T1 - The aromatic peroxygenase from Marasmius rutola-a new enzyme for biosensor applications JF - Analytical & bioanalytical chemistry N2 - 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. KW - Unspecific peroxygenase KW - Cytochrome P450 KW - Biosensors KW - Phenolic substances Y1 - 2012 U6 - https://doi.org/10.1007/s00216-011-5497-y SN - 1618-2642 VL - 402 IS - 1 SP - 405 EP - 412 PB - Springer CY - Heidelberg 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 -