@article{WernerGroebelSchuhmacheretal.2009,
  author    = {Werner, Frederik and Groebel, Simone and Schuhmacher, K. and Spelthahn, Heiko and Wagner, Torsten and Selmer, Thorsten and Baumann, Marcus and Sch{\"o}ning, Michael Josef},
  title     = {Bestimmung der metabolischen Aktivit{\"a}t von Mikroorganismen w{\"a}hrend des Biogasbildungsprozesses},
  series = {9. Dresdner Sensor-Symposium : Dresden, 07.-09. Dezember 2009 / Gerlach, Gerald ; Hauptmann, Peter [Hrsg.]},
  journal   = {9. Dresdner Sensor-Symposium : Dresden, 07.-09. Dezember 2009 / Gerlach, Gerald ; Hauptmann, Peter [Hrsg.]},
  publisher = {TUDpress},
  address   = {Dresden},
  isbn      = {978-3-941298-44-6},
  pages     = {201 -- 204},
  year      = {2009},
  language  = {de}
}
@article{WernerKrumbeSchumacheretal.2011,
  author    = {Werner, Frederik and Krumbe, Christoph and Schumacher, Katharina and Groebel, Simone and Spelthahn, Heiko and Stellberg, Michael and Wagner, Torsten and Yoshinobu, Tatsuo and Selmer, Thorsten and Keusgen, Michael and Baumann, Marcus and Sch{\"o}ning, Michael Josef},
  title     = {Determination of the extracellular acidification of Escherichia coli by a light-addressable potentiometric sensor},
  series = {Physica status solidi (a) : applications and material science. 208 (2011), H. 6},
  journal   = {Physica status solidi (a) : applications and material science. 208 (2011), H. 6},
  publisher = {Wiley},
  address   = {Weinheim},
  isbn      = {1862-6319},
  pages     = {1340 -- 1344},
  year      = {2011},
  language  = {en}
}
@article{WernerGroebelWagneretal.2011,
  author    = {Werner, Frederik and Groebel, Simone and Wagner, Torsten and Yoshinobu, Tatsuo and Selmer, Thorsten and Baumann, Marcus and Sch{\"o}ning, Michael Josef},
  title     = {{\"U}berwachung der metabolischen Aktivit{\"a}t von Mikroorganismen zur Kontrolle des biologischen Prozesses im Biogasfermenter},
  series = {Biogas 2011 : Energietr{\"a}ger der Zukunft ; 6. Fachtagung, Fachtagung Braunschweig, 08. und 09. Juni 2011 / VDI Energie und Umwelt},
  journal   = {Biogas 2011 : Energietr{\"a}ger der Zukunft ; 6. Fachtagung, Fachtagung Braunschweig, 08. und 09. Juni 2011 / VDI Energie und Umwelt},
  publisher = {VDI-Verl.},
  address   = {D{\"u}sseldorf},
  isbn      = {978-3-18-092121-1},
  pages     = {285 -- 286},
  year      = {2011},
  language  = {de}
}
@article{WernerGroebelKrumbeetal.2012,
  author    = {Werner, Frederik and Groebel, Simone and Krumbe, Christoph and Wagner, Torsten and Selmer, Thorsten and Yoshinobu, Tatsuo and Baumann, Marcus and Sch{\"o}ning, Michael Josef},
  title     = {Nutrient concentration-sensitive microorganism-based biosensor},
  series = {Physica Status Solidi (a)},
  volume    = {209},
  journal   = {Physica Status Solidi (a)},
  number    = {5},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1862-6319},
  doi       = {10.1002/pssa.201100801},
  pages     = {900 -- 904},
  year      = {2012},
  language  = {en}
}
@article{SchiffelsPinkenburgScheldenetal.2013,
  author    = {Schiffels, Johannes and Pinkenburg, Olaf and Schelden, Maximilian and Aboulnaga, El-Hussiny A. A. and Baumann, Marcus and Selmer, Thorsten},
  title     = {An innovative cloning platform enables large-scale production and maturation of an oxygen-tolerant [NiFe]-hydrogenase from cupriavidus necator in Escherichia coli},
  series = {PLOS one. 2013},
  journal   = {PLOS one. 2013},
  publisher = {Public Library of Science},
  address   = {San Francisco, California},
  issn      = {1932-6203},
  doi       = {10.1371/journal.pone.0068812},
  year      = {2013},
  language  = {en}
}
@article{AbulnagaPinkenburgSchiffelsetal.2013,
  author    = {Abulnaga, El-Hussiny and Pinkenburg, Olaf and Schiffels, Johannes and E-Refai, Ahmed and Buckel, Wolfgang and Selmer, Thorsten},
  title     = {Effect of an Oxygen-Tolerant Bifurcating Butyryl Coenzyme A Dehydrogenase/Electron-Transferring Flavoprotein Complex from Clostridium difficile on Butyrate Production in Escherichia coli},
  series = {Journal of bacteriology},
  volume    = {195},
  journal   = {Journal of bacteriology},
  number    = {16},
  issn      = {1098-5530 [E-Journal]},
  pages     = {3704 -- 3713},
  year      = {2013},
  language  = {en}
}
@article{HeineHerrmannSelmeretal.2014,
  author    = {Heine, A. and Herrmann, G. and Selmer, Thorsten and Terwesten, F. and Buckel, W. and Reuter, K.},
  title     = {High resolution crystal structure of clostridium propionicum β-Alanyl-CoA:Ammonia Lyase, a new member of the "Hot Dog Fold" protein superfamily},
  series = {Proteins},
  volume    = {82},
  journal   = {Proteins},
  number    = {9},
  publisher = {Wiley-Liss},
  address   = {New York},
  issn      = {1097-0134 (E-Journal); 0887-3585 (Print)},
  doi       = {10.1002/prot.24557},
  pages     = {2041 -- 2053},
  year      = {2014},
  abstract  = {Clostridium propionicum is the only organism known to ferment β-alanine, a constituent of coenzyme A (CoA) and the phosphopantetheinyl prosthetic group of holo-acyl carrier protein. The first step in the fermentation is a CoA-transfer to β-alanine. Subsequently, the resulting β-alanyl-CoA is deaminated by the enzyme β-alanyl-CoA:ammonia lyase (Acl) to reversibly form ammonia and acrylyl-CoA. We have determined the crystal structure of Acl in its apo-form at a resolution of 0.97 {\AA} as well as in complex with CoA at a resolution of 1.59 {\AA}. The structures reveal that the enyzme belongs to a superfamily of proteins exhibiting a so called "hot dog fold" which is characterized by a five-stranded antiparallel β-sheet with a long α-helix packed against it. The functional unit of all "hot dog fold" proteins is a homodimer containing two equivalent substrate binding sites which are established by the dimer interface. In the case of Acl, three functional dimers combine to a homohexamer strongly resembling the homohexamer formed by YciA-like acyl-CoA thioesterases. Here, we propose an enzymatic mechanism based on the crystal structure of the Acl·CoA complex and molecular docking. Proteins 2014; 82:2041-2053. © 2014 Wiley Periodicals, Inc.},
  language  = {en}
}
@article{SchoeningBiselliSelmeretal.2012,
  author    = {Sch{\"o}ning, Michael Josef and Biselli, Manfred and Selmer, Thorsten and {\"O}hlschl{\"a}ger, Peter and Baumann, Marcus and F{\"o}rster, Arnold and Poghossian, Arshak},
  title     = {Forschung „zwischen" den Disziplinen: das Institut f{\"u}r Nano- und Biotechnologien},
  series = {Analytik news : das Online-Labormagazin f{\"u}r Labor und Analytik},
  volume    = {Publ. online},
  journal   = {Analytik news : das Online-Labormagazin f{\"u}r Labor und Analytik},
  publisher = {Dr. Beyer Internet-Beratung},
  address   = {Ober-Ramstadt},
  pages     = {11 Seiten},
  year      = {2012},
  abstract  = {"Biologie trifft Mikroelektronik", das Motto des Instituts f{\"u}r Nano- und Biotechnologien (INB) an der FH Aachen, unterstreicht die zunehmende Bedeutung interdisziplin{\"a}r gepr{\"a}gter Forschungsaktivit{\"a}ten. Der thematische Zusammenschluss grundst{\"a}ndiger Disziplinen, wie die Physik, Elektrotechnik, Chemie, Biologie sowie die Materialwissenschaften, l{\"a}sst neue Forschungsgebiete entstehen, ein herausragendes Beispiel hierf{\"u}r ist die Nanotechnologie: Hier werden neue Werkstoffe und Materialien entwickelt, einzelne Nanopartikel oder Molek{\"u}le und deren Wechselwirkung untersucht oder Schichtstrukturen im Nanometerbereich aufgebaut, die neue und vorher nicht bekannte Eigenschaften hervorbringen. Vor diesem Hintergrund b{\"u}ndelt das im Jahre 2006 gegr{\"u}ndete INB die an der FH Aachen vorhandenen Kompetenzen von derzeit insgesamt sieben Laboratorien auf den Gebieten der Halbleitertechnik und Nanoelektronik, Nanostrukturen und DNA-Sensorik, der Chemo- und Biosensorik, der Enzymtechnologie, der Mikrobiologie und Pflanzenbiotechnologie, der Zellkulturtechnik, sowie der Roten Biotechnologie synergetisch. In der Nano- und Biotechnologie steckt außergew{\"o}hnliches Potenzial! Nicht zuletzt deshalb stellen sich die Forscher der Herausforderung, in diesem Bereich gemeinsam zu forschen und Schnittstellen zu nutzen, um so bei der Gestaltung neuartiger Ideen und Produkte mitzuwirken, die zuk{\"u}nftig unser allt{\"a}gliches Leben ver{\"a}ndern werden. Im Folgenden werden die verschiedenen Forschungsbereiche kurz zusammenfassend vorgestellt und vorhandene Interaktionen anhand von exemplarisch ausgew{\"a}hlten, aktuellen Forschungsprojekten skizziert.},
  language  = {de}
}
@article{PilasIkenSelmeretal.2015,
  author    = {Pilas, Johanna and Iken, Heiko and Selmer, Thorsten and Keusgen, Michael and Sch{\"o}ning, Michael Josef},
  title     = {Development of a multi-parameter sensor chip for the simultaneous detection of organic compounds in biogas processes},
  series = {Physica status solidi (a)},
  volume    = {212},
  journal   = {Physica status solidi (a)},
  number    = {6},
  publisher = {Wiley},
  address   = {Weinheim},
  issn      = {1862-6319},
  doi       = {10.1002/pssa.201431894},
  pages     = {1306 -- 1312},
  year      = {2015},
  abstract  = {An enzyme-based multi-parameter biosensor is developed for monitoring the concentration of formate, d-lactate, and l-lactate in biological samples. The sensor is based on the specific dehydrogenation by an oxidized β-nicotinamide adenine dinucleotide (NAD+)-dependent dehydrogenase (formate dehydrogenase, d-lactic dehydrogenase, and l-lactic dehydrogenase, respectively) in combination with a diaphorase from Clostridium kluyveri (EC 1.8.1.4). The enzymes are immobilized on a platinum working electrode by cross-linking with glutaraldehyde (GA). The principle of the determination scheme in case of l-lactate is as follows: l-lactic dehydrogenase (l-LDH) converts l-lactate into pyruvate by reaction with NAD+. In the presence of hexacyanoferrate(III), the resulting reduced β-nicotinamide adenine dinucleotide (NADH) is then regenerated enzymatically by diaphorase. The electrochemical detection is based on the current generated by oxidation of hexacyanoferrate(II) at an applied potential of +0.3 V vs. an Ag/AgCl reference electrode. The biosensor will be electrochemically characterized in terms of linear working range and sensitivity. Additionally, the successful practical application of the sensor is demonstrated in an extract from maize silage.},
  language  = {en}
}
@article{SchiffelsSelmer2015,
  author    = {Schiffels, Johannes and Selmer, Thorsten},
  title     = {A flexible toolbox to study protein-assisted metalloenzyme assembly in vitro},
  series = {Biotechnology and Bioengineering},
  volume    = {112},
  journal   = {Biotechnology and Bioengineering},
  number    = {11},
  publisher = {Wiley},
  address   = {Weinheim},
  issn      = {1097-0290},
  doi       = {10.1002/bit.25658},
  pages     = {2360 -- 2372},
  year      = {2015},
  language  = {en}
}