@inproceedings{GroebelWernerJoerresetal.2011,
  author    = {Groebel, Simone and Werner, Frederik and J{\"o}rres, Niklas and Jansen, F. and Kasper, Katharina and Schiffels, Johannes and Sprenger, B. and Baumann, Marcus and Sch{\"o}ning, Michael Josef and Selmer, Thorsten},
  title     = {Entwicklung einer Sensor-{\"U}berwachung f{\"u}r Biogasanlagen auf Basis von Prozessdaten einer Parallelanlage},
  series = {10. Dresdner Sensor-Symposium : Dresden, 5. - 7. Dezember 2011 ; miniaturisierte analytische Verfahren, Hochtemperatur-Sensoren, Sensoren f{\"u}r Bioprozess- und Verfahrenstechnik, Sensoren f{\"u}r die Medizin, Chemische Verfahrenstechnik, Lebensmittelanalytik, innovative Sensorl{\"o}sungen, Sensoren f{\"u}r die Wasserqualit{\"a}t, Selbst{\"u}berwachung / Gerald Gerlach ... (Hg.)},
  booktitle = {10. Dresdner Sensor-Symposium : Dresden, 5. - 7. Dezember 2011 ; miniaturisierte analytische Verfahren, Hochtemperatur-Sensoren, Sensoren f{\"u}r Bioprozess- und Verfahrenstechnik, Sensoren f{\"u}r die Medizin, Chemische Verfahrenstechnik, Lebensmittelanalytik, innovative Sensorl{\"o}sungen, Sensoren f{\"u}r die Wasserqualit{\"a}t, Selbst{\"u}berwachung / Gerald Gerlach ... (Hg.)},
  publisher = {TUDpress},
  address   = {Dresden},
  isbn      = {978-3-942710-53-4},
  doi       = {10.5162/10dss2011/4.3},
  pages     = {81 -- 84},
  year      = {2011},
  abstract  = {Beim Ausbau nachhaltiger, regenerativer Energieversorgung hat die Umwandlung von organischer Biomasse in Biogas ein großes Potential. Der zugrundeliegende, komplexe biologische Prozess wird noch immer unzureichend verstanden und bedarf systematischer Untersuchungen der Prozessparameter, um einen hohen Ertrag bei guter Gasqualit{\"a}t zu erm{\"o}glichen. Die Fragestellungen zur Entschl{\"u}sselung des Prozesses sind sowohl verfahrenstechnischer als auch mikrobiologischer Natur. Aus mikrobiologischer Sicht ist die Kenntnis der tats{\"a}chlich beteiligten prozesstragenden Mikroorganismen von erheblicher Bedeutung, aus verfahrenstechnischer Sicht die Kenntnis der physikalischen und chemischen Faktoren, welche die mikrobiologischen Prozesse und kontrollieren. Im Zusammenspiel aller dieser Parameter wird die Biogasbildung bef{\"o}rdert oder behindert, bis zum Abbruch des Prozesses. Eine m{\"o}gliche Kontrollmethode ist die Messung der metabolischen Aktivit{\"a}t prozesstragender Organismen. Diese soll, beruhend auf fundierten Prozessdaten, gewonnen durch eine Parallelanlage, mit einem lichtadressierbaren potentiometrischen Sensor-System (LAPS) realisiert werden. Dieser Sensor ist in der Lage, pH-Wert-{\"a}nderungen zu detektieren, die durch den Stoffwechsel der auf dem Chip immobilisierten Organismen hervorgerufen werden, um eine Online-{\"U}berwachung von Biogasanlagen zu erm{\"o}glichen.},
  language  = {de}
}
@article{SelmerJennemannBaueretal.1999,
  author    = {Selmer, Thorsten and Jennemann, Richard and Bauer, Bernhard L. and Bertalanffy, Helmut},
  title     = {Novel glycoinositolphosphosphingolipids, basidiolipids, from Agaricus / Jennemann, Richard ; Bauer, Bernhard, L. ; Bertalanffy, Helmut ; Geyer, Rudolf ; Gschwind, Ruth, M. ; Selmer, Thorsten ; Wiegandt, Herbert},
  series = {European Journal of Biochemistry. 259 (1999), H. 1-2},
  journal   = {European Journal of Biochemistry. 259 (1999), H. 1-2},
  isbn      = {0014-2956},
  pages     = {331 -- 338},
  year      = {1999},
  language  = {en}
}
@article{SelmerHallmannSchmidtetal.1996,
  author    = {Selmer, Thorsten and Hallmann, Armin and Schmidt, Bernhard and Sumper, Manfred},
  title     = {The Evolutionary Conservation of a Novel Protein Modification, the Conversion of Cysteine to Serinesemialdehyde in Arylsulfatase from Volvox carteri / Selmer, Thorsten ; Hallmann, Armin ; Schmidt, Bernhard ; Sumper, Manfred ; Figura, Kurt von},
  series = {European Journal of Biochemistry. 238 (1996), H. 2},
  journal   = {European Journal of Biochemistry. 238 (1996), H. 2},
  isbn      = {0014-2956},
  pages     = {341 -- 345},
  year      = {1996},
  language  = {en}
}
@article{SelmerScottNaeseretal.2004,
  author    = {Selmer, Thorsten and Scott, Richard and N{\"a}ser, Ulrike and Friedrich, Peter},
  title     = {Stereochemistry of hydrogen removal from the 'unactivated' C-3 position of 4-hydroxybutyryl-CoA catalysed by 4-hydroxybutyryl-CoA dehydratase / Scott, R. ; N{\"a}ser, U. ; Friedrich, P. ; Selmer, T. ; Buckel, W. ; Golding, BT.},
  series = {Chemical Communications : ChemCom (2004)},
  journal   = {Chemical Communications : ChemCom (2004)},
  isbn      = {1364-548X},
  pages     = {1210 -- 1211},
  year      = {2004},
  language  = {en}
}
@article{SelmerThamerCirpusetal.2003,
  author    = {Selmer, Thorsten and Thamer, Wiebke and Cirpus, Irina and Hans, Marcus},
  title     = {A two [4Fe-4S]-cluster-containing ferredoxin as an alternative electron donor for 2-hydroxyglutaryl-CoA dehydratase from Acidaminococcus fermentans / Thamer, Wiebke ; Cirpus, Irina ; Hans, Marcus ; Pierik, Antonio, J. ; Selmer, Thorsten ; Bill, Eckhard ;},
  series = {Archives of Microbiology. 179 (2003), H. 3},
  journal   = {Archives of Microbiology. 179 (2003), H. 3},
  isbn      = {1432-072X},
  pages     = {197 -- 204},
  year      = {2003},
  language  = {en}
}
@article{SelmerNetzPohletal.2002,
  author    = {Selmer, Thorsten and Netz, Daili Jacqueline Aguilar and Pohl, Regula and Beck-Sickinger, Annette G.},
  title     = {Biochemical characterisation and genetic analysis of aureocin A53, a new, atypical bacteriocin from Staphylococcus aureus / Netz, Daili Jacqueline Aguilar ; Pohl, Regula ; Beck-Sickinger, Annette G. ; Selmer, Thorsten ; Pierik, Antonio J. ; Carmo de Frei},
  series = {Journal of Molecular Biology. 319 (2002), H. 3},
  journal   = {Journal of Molecular Biology. 319 (2002), H. 3},
  isbn      = {0022-2836},
  pages     = {745 -- 756},
  year      = {2002},
  language  = {en}
}
@article{SelmerSchmidtIngendohetal.1995,
  author    = {Selmer, Thorsten and Schmidt, Bernhard and Ingendoh, Arnd and Figura, Kurt von},
  title     = {A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency / Schmidt, Bernhard ; Selmer, Thorsten ; Ingendoh, Arnd ; Figurat, Kurt von},
  series = {Cell. 82 (1995), H. 2},
  journal   = {Cell. 82 (1995), H. 2},
  isbn      = {0092-8674},
  pages     = {271 -- 278},
  year      = {1995},
  language  = {en}
}
@article{SelmerKahntGoubeaudetal.2000,
  author    = {Selmer, Thorsten and Kahnt, J{\"o}rg and Goubeaud, Marcel and Shima, Seigo},
  title     = {The biosynthesis of methylated amino acids in the active site region of methyl-coenzyme M reductase / Selmer, Thorsten ; Kahnt, J{\"o}rg ; Goubeaud, Marcel ; Shima, Seigo ; Grabarse, Wolfgang ; Ermler, Ulrich ; Thauer, Rudolf K.},
  series = {Journal of Biological Chemistry. 275 (2000), H. 6},
  journal   = {Journal of Biological Chemistry. 275 (2000), H. 6},
  isbn      = {1083-351X},
  pages     = {3775 -- 3760},
  year      = {2000},
  language  = {en}
}
@article{SelmerBrueserDahl2000,
  author    = {Selmer, Thorsten and Br{\"u}ser, Thomas and Dahl, Christiane},
  title     = {ADP Sulfurylase" from Thiobacillus denitrificans Is an Adenylylsulfate:Phosphate Adenylyltransferase and Belongs to a New Family of Nucleotidyltransferases / Br{\"u}ser, Thomas ; Selmer, Thorsten ; Dahl, Christiane},
  series = {Journal of Biological Chemistry. 275 (2000), H. 3},
  journal   = {Journal of Biological Chemistry. 275 (2000), H. 3},
  isbn      = {1083-351X},
  pages     = {1691 -- 1690},
  year      = {2000},
  language  = {en}
}
@article{SelmerBuckel1999,
  author    = {Selmer, Thorsten and Buckel, Wolfgang},
  title     = {Oxygen Exchange between Acetate and the Catalytic Glutamate Residue in Glutaconate CoA-transferase from Acidaminococcus fermentans. IMPLICATIONS FOR THE MECHANISM OF CoA-ESTER HYDROLYSIS},
  series = {Journal of Biological Chemistry. 274 (1999), H. 30},
  journal   = {Journal of Biological Chemistry. 274 (1999), H. 30},
  isbn      = {1083-351X},
  pages     = {20772 -- 20778},
  year      = {1999},
  language  = {en}
}
@article{SelmerRecksiekDierksetal.1998,
  author    = {Selmer, Thorsten and Recksiek, Michael and Dierks, Thomas and Schmidt, Bernhard},
  title     = {Sulfatases, Trapping of the Sulfated Enzyme Intermediate by Substituting the Active Site Formylglycine / Recksiek, Michael ; Selmer, Thorsten ; Dierks, Thomas ; Schmidt, Bernhard ; Figura, Kurt von},
  series = {Journal of Biological Chemistry. 273 (1998), H. 11},
  journal   = {Journal of Biological Chemistry. 273 (1998), H. 11},
  isbn      = {1083-351X},
  pages     = {6096 -- 6103},
  year      = {1998},
  language  = {en}
}
@article{SelmerMiechDierksetal.1998,
  author    = {Selmer, Thorsten and Miech, Claudia and Dierks, Thomas and Figura, Kurt von},
  title     = {Arylsulfatase from Klebsiella pneumoniae Carries a Formylglycine Generated from a Serine / Miech, Claudia ; Dierks, Thomas ; Selmer, Thorsten ; Figura, Kurt von ; Schmidt, Bernd},
  series = {Journal of Biological Chemistry. 273 (1998), H. 9},
  journal   = {Journal of Biological Chemistry. 273 (1998), H. 9},
  isbn      = {1083-351X},
  pages     = {4835 -- 4837},
  year      = {1998},
  language  = {en}
}
@article{SelmerSommerladeIngendohetal.1994,
  author    = {Selmer, Thorsten and Sommerlade, Hans-J{\"o}rg and Ingendoh, Arnd and Gieselmann, Volkmar},
  title     = {Glycosylation and phosphorylation of arylsulfatase A / Sommerlade, Hans-J{\"o}rg. ; Selmer, Thomas. ; Ingendoh, Arnd ; Gieselmann, Volkmar ; Figura, Kurt von ; Neifer, Klaus ; Schmidt, Bernhard},
  series = {Journal of Biological Chemistry. 269 (1994), H. 33},
  journal   = {Journal of Biological Chemistry. 269 (1994), H. 33},
  isbn      = {1083-351X},
  pages     = {20977 -- 20981},
  year      = {1994},
  language  = {en}
}
@article{SelmerJennemannBaueretal.1999,
  author    = {Selmer, Thorsten and Jennemann, Richard and Bauer, Bernhard L. and Bertalanffy, Helmut},
  title     = {Basidiolipids from Agaricus are novel immune adjuvants / Jennemann, R. ; Bauer, BL. ; Bertalanffy, H. ; Selmer, T. ; Wiegandt, H.},
  series = {Immunobiology. 200 (1999), H. 2},
  journal   = {Immunobiology. 200 (1999), H. 2},
  isbn      = {0171-2985},
  pages     = {277 -- 289},
  year      = {1999},
  language  = {en}
}
@article{SelmerFiguraSchmidtetal.1998,
  author    = {Selmer, Thorsten and Figura, Kurt von and Schmidt, Bernhard and Dierks, T.},
  title     = {A novel protein modification generating an aldehyde group in sulfatases: its role in catalysis and disease / Figura, Kurt von ; Schmidt, Bernhard ; Selmer, Thorsten ; Dierks, Thomas},
  series = {Bioessays. 20 (1998), H. 6},
  journal   = {Bioessays. 20 (1998), H. 6},
  isbn      = {1521-1878},
  pages     = {505 -- 510},
  year      = {1998},
  language  = {en}
}
@article{SelmerLukatelaKraussetal.1998,
  author    = {Selmer, Thorsten and Lukatela, G. and Krauss, N. and Theis, K.},
  title     = {Crystal structure of human arylsulfatase A: the aldehyde function and the metal ion at the active site suggest a novel mechanism for sulfate ester hydrolysis / Lukatela, G. ; Krauss, N. ; Theis, K. ; Selmer, T. ; Gieselmann, V. ; Figura, K. von ; Saenger,},
  series = {Biochemistry. 37 (1998), H. 11},
  journal   = {Biochemistry. 37 (1998), H. 11},
  pages     = {3654 -- 3664},
  year      = {1998},
  language  = {en}
}
@article{SelmerKimDarleyetal.2006,
  author    = {Selmer, Thorsten and Kim, Jihoe and Darley, Daniel and Buckel, Wolfgang},
  title     = {Characterization of (R)-2-hydroxyisocaproate dehydrogenase and a family III coenzyme A transferase involved in reduction of L-leucine to isocaproate by Clostridium difficile / Kim, J. ; Darley, D. ; Selmer, T. ; Buckel, W.},
  series = {Applied and Environmental Microbiology. 72 (2006), H. 9},
  journal   = {Applied and Environmental Microbiology. 72 (2006), H. 9},
  isbn      = {0099-2240},
  pages     = {6062 -- 6069},
  year      = {2006},
  language  = {en}
}
@article{SelmerYuBlaseretal.2006,
  author    = {Selmer, Thorsten and Yu, Lihua and Blaser, Martin and Andrei, Paula I.},
  title     = {4-Hydroxyphenylacetate decarboxylases: properties of a novel subclass of glycyl radical enzyme systems / Yu, L. ; Blaser, M. ; Andrei, PI. ; Pierik, AJ. Selmer, T.},
  series = {Biochemistry. 31 (2006), H. 45},
  journal   = {Biochemistry. 31 (2006), H. 45},
  pages     = {9584 -- 9592},
  year      = {2006},
  language  = {en}
}
@article{SelmerPierikHeider2005,
  author    = {Selmer, Thorsten and Pierik, Antonio J. and Heider, Johann},
  title     = {New glycyl radical enzymes catalysing key metabolic steps in anaerobic bacteria},
  series = {Biological Chemistry. 386 (2005), H. 10},
  journal   = {Biological Chemistry. 386 (2005), H. 10},
  isbn      = {1431-6730},
  pages     = {981 -- 988},
  year      = {2005},
  language  = {en}
}
@article{SelmerAchebachUnden2005,
  author    = {Selmer, Thorsten and Achebach, Stephanie and Unden, Gottfried},
  title     = {Properties and significance of apoFNR as a second form of air-inactivated [4Fe-4S]·FNR of Escherichia coli / Achebach, S. ; Selmer, T. ; Unden, G.},
  series = {The FEBS Journal. 272 (2005), H. 16},
  journal   = {The FEBS Journal. 272 (2005), H. 16},
  isbn      = {1742-464X},
  pages     = {4260 -- 4269},
  year      = {2005},
  language  = {en}
}
@article{SelmerHermannJessenetal.2005,
  author    = {Selmer, Thorsten and Hermann, Gloria and Jessen, Holly and Gokarn, Ravi R.},
  title     = {Two beta-alanyl-CoA:ammonia lyases in Clostridium propionicum / Herrmann , G. ; Selmer, T. ; Jessen, HJ. ; Gokarn, RR. ; Selifonova, O. ; Gort , SJ. ; , Buckel, W.},
  series = {The FEBS Journal. 272 (2005), H. 3},
  journal   = {The FEBS Journal. 272 (2005), H. 3},
  isbn      = {1742-464X},
  pages     = {813 -- 821},
  year      = {2005},
  language  = {en}
}
@article{SelmerAndreiPieriketal.2004,
  author    = {Selmer, Thorsten and Andrei, Paula I. and Pierik, Antonio J. and Zauner, Stefan},
  title     = {Subunit composition of the glycyl radical enzyme p-hydroxyphenylacetate decarboxylase. A small subunit, HpdC, is essential for catalytic activity / Andrei, PI. ; Pierik, AJ. ; Zauner , S. ; Andrei-Selmer, LC. ; Selmer, T.},
  series = {European Journal of Biochemistry. 271 (2004), H. 11},
  journal   = {European Journal of Biochemistry. 271 (2004), H. 11},
  isbn      = {0014-2956},
  pages     = {2225 -- 2230},
  year      = {2004},
  language  = {en}
}
@article{SelmerHetzelBrocketal.2003,
  author    = {Selmer, Thorsten and Hetzel, Marc and Brock, Matthias and Pierik, Antonio J.},
  title     = {Acryloyl-CoA reductase from Clostridium propionicum. An enzyme complex of propionyl-CoA dehydrogenase and electron-transferring flavoprotein / Hetzel, Marc ; Brock, Matthias ; Selmer, Thorsten, Pierik, Antonio J. ; Golding, Bernard T. ; Buckel, Wolfgang},
  series = {European Journal of Biochemistry. 270 (2003), H. 5},
  journal   = {European Journal of Biochemistry. 270 (2003), H. 5},
  isbn      = {0014-2956},
  pages     = {902 -- 910},
  year      = {2003},
  language  = {en}
}
@article{SelmerWillanzheimerHetzel2002,
  author    = {Selmer, Thorsten and Willanzheimer, Angela and Hetzel, Marc},
  title     = {Propionate CoA-transferase from Clostridium propionicum. Cloning of the gene and identification of glutamate 324 at the active site},
  series = {European Journal of Biochemistry. 269 (2002), H. 1},
  journal   = {European Journal of Biochemistry. 269 (2002), H. 1},
  isbn      = {0014-2956},
  pages     = {372 -- 380},
  year      = {2002},
  language  = {en}
}
@article{SelmerAndrei2001,
  author    = {Selmer, Thorsten and Andrei, Paula I.},
  title     = {p-Hydroxyphenylacetate decarboxylase from Clostridium difficile. A novel glycyl radical enzyme catalysing the formation of p-cresol},
  series = {European Journal of Biochemistry. 268 (2001), H. 5},
  journal   = {European Journal of Biochemistry. 268 (2001), H. 5},
  isbn      = {0014-2956},
  pages     = {1363 -- 1372},
  year      = {2001},
  language  = {en}
}
@article{SelmerDarleyCleggetal.2003,
  author    = {Selmer, Thorsten and Darley, Dan J. and Clegg, William and Harrington, Ross W.},
  title     = {Stereocontrolled Synthesis of (2R,3S)-2-Methylisocitrate, a Central Intermediate in the Methylcitrate Cycle / Darley, Dan J. ; Selmer, Thorsten ; Clegg, William ; Harrington, Ross W. ; Buckel, Wolfgang ; Golding, Bernardt},
  series = {Helvetica chimica acta. 86 (2003), H. 12},
  journal   = {Helvetica chimica acta. 86 (2003), H. 12},
  isbn      = {1522-2675},
  pages     = {3991 -- 3999},
  year      = {2003},
  language  = {en}
}
@book{Selmer1996,
  author    = {Selmer, Thorsten},
  title     = {Nachweis einer neuartigen posttranslationalen Modifikation in Sulfatasen und ihr Fehlen in Enzymen aus Patienten mit multipler Sulfatase-Defizienz},
  publisher = {Cuvillier},
  address   = {G{\"o}ttingen},
  pages     = {XIII, 143, IX S. : graph. Darst.},
  year      = {1996},
  language  = {de}
}
@article{BalakrishnanAndreiSelmerSelmeretal.2010,
  author    = {Balakrishnan, Karthikeyan and Andrei-Selmer, Luminita-Cornelia and Selmer, Thorsten and Bacher, Michael and Dodel, Richard},
  title     = {Comparison of Intravenous Immunoglobulins for Naturally Occurring Autoantibodies against Amyloid-β},
  series = {Journal of Alzheimer's Disease},
  volume    = {20},
  journal   = {Journal of Alzheimer's Disease},
  number    = {1},
  isbn      = {1387-2877},
  pages     = {135 -- 143},
  year      = {2010},
  language  = {en}
}
@article{SelmerPinkenburg2008,
  author    = {Selmer, Thorsten and Pinkenburg, Olaf},
  title     = {Method of cloning at least one nucleic acid molecule of interest using type IIS restriction endonucleases, and corresponding cloning vectors, kits and system using type IIS restriction endonucleases / Selmer, Thorsten ; Pinkenburg, Olaf},
  year      = {2008},
  language  = {en}
}
@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{MartinsBlaserFeliksetal.2011,
  author    = {Martins, Berta M. and Blaser, Martin and Feliks, Mikolaj and Ullmann, Matthias G. and Buckel, Wolfgang and Selmer, Thorsten},
  title     = {Structural basis for a Kolbe-type decarboxylation catalyzed by a glycyl radical enzyme},
  series = {Journal of the American Chemical Society},
  journal   = {Journal of the American Chemical Society},
  publisher = {ACS Publications},
  address   = {Washington, DC},
  pages     = {1 -- 33},
  year      = {2011},
  language  = {en}
}
@article{SchiffelsBaumannSelmer2011,
  author    = {Schiffels, Johannes and Baumann, Marcus and Selmer, Thorsten},
  title     = {Facile analysis of short-chain fatty acids as 4-nitrophenyl esters in complex anaerobic fermentation samples by high performance liquid chromatography},
  series = {Journal of Chromatography A. 1218 (2011), H. 34},
  journal   = {Journal of Chromatography A. 1218 (2011), H. 34},
  publisher = {Elsevier},
  address   = {Amsterdam},
  isbn      = {0021-9673},
  pages     = {5848 -- 5851},
  year      = {2011},
  language  = {en}
}
@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{AboulnagaPinkenburgSchiffelsetal.2013,
  author    = {Aboulnaga, E. H. and Pinkenburg, O. and Schiffels, Johannes and El-Refai, A. and Buckel, W. and Selmer, Thorsten},
  title     = {Butyrate production in Escherichia coli: Exploitation of an oxygen tolerant bifurcating butyryl-CoA dehydrogenase/electron transferring flavoprotein complex from Clostridium difficile},
  series = {Journal of bacteriology. June 14, 2013},
  journal   = {Journal of bacteriology. June 14, 2013},
  issn      = {1098-5530 (E-Journal) ; 0021-9193 (Print)},
  pages     = {Epub ahead of print},
  year      = {2013},
  language  = {de}
}
@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}
}
@techreport{SchoeningSelmerBaumann2012,
  author    = {Sch{\"o}ning, Michael Josef and Selmer, Thorsten and Baumann, Marcus},
  title     = {Schlussbericht zum Projekt "Bio-LAPS" : Optimierung des Betriebs eines Biogasfermenters mit Hilfe eines Feldeffekt-Biosensors auf Basis eines lichtadressierbaren potentiometrischen Sensors (LAPS) : Laufzeit: 01.09.2008 bis 31.01.2012 : F{\"o}rderkennzeichen 07NR264 bzw.22026407},
  publisher = {BMELV},
  address   = {Berlin},
  pages     = {44 S.},
  year      = {2012},
  language  = {de}
}
@inproceedings{KasparGroebelKuperjansetal.2013,
  author    = {Kaspar, K. and Groebel, Simone and Kuperjans, Isabel and Dielmann, Klaus-Peter and Selmer, Thorsten},
  title     = {Charakterisierung der Bioz{\"o}nose von Biogasfermentern in Abh{\"a}ngigkeit verschiedener Substrate},
  series = {Biogas 2013 : 6. Innovationskongress, 23. - 24.05.2013, Osnabr{\"u}ck, Tagungsband},
  booktitle = {Biogas 2013 : 6. Innovationskongress, 23. - 24.05.2013, Osnabr{\"u}ck, Tagungsband},
  publisher = {Profair Consult+Project},
  address   = {Hildesheim},
  issn      = {978-3-9813776-3-7},
  pages     = {69 -- 74},
  year      = {2013},
  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}
}
@article{PilasMarianoKeusgenetal.2015,
  author    = {Pilas, Johanna and Mariano, K. and Keusgen, M. and Selmer, Thorsten and Sch{\"o}ning, Michael Josef},
  title     = {Optimization of an Enzyme-based Multi-parameter Biosensor for Monitoring Biogas Processes},
  series = {Procedia Engineering},
  volume    = {120},
  journal   = {Procedia Engineering},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {1877-7058},
  doi       = {10.1016/j.proeng.2015.08.702},
  pages     = {532 -- 535},
  year      = {2015},
  language  = {en}
}
@inproceedings{KasperSchiffelsKrafftetal.2016,
  author    = {Kasper, Katharina and Schiffels, Johannes and Krafft, Simone and Kuperjans, Isabel and Elbers, Gereon and Selmer, Thorsten},
  title     = {Biogas Production on Demand Regulated by Butyric Acid Addition},
  series = {IOP Conference Series: Earth and Environmental Science. Bd. 32},
  volume    = {32},
  booktitle = {IOP Conference Series: Earth and Environmental Science. Bd. 32},
  issn      = {1755-1315},
  doi       = {10.1088/1755-1315/32/1/012009},
  pages     = {012009/1 -- 012009/4},
  year      = {2016},
  language  = {en}
}
@article{PinkenburgSchiffelsSelmer2016,
  author    = {Pinkenburg, Olaf and Schiffels, Johannes and Selmer, Thorsten},
  title     = {Das CoLibry-Konzept - ein Werkzeugkasten f{\"u}r die Synthetische Biologie: Bioproduktion},
  series = {BIOspektrum},
  volume    = {22},
  journal   = {BIOspektrum},
  number    = {6},
  publisher = {Springer},
  address   = {Berlin},
  doi       = {10.1007/s12268-016-0734-8},
  pages     = {593 -- 595},
  year      = {2016},
  abstract  = {Regardless of size or destination, synthetic biology starts with com-parably small information units, which need to be combined and properly arranged in order to achieve a certain goal. This may be the de novo synthesis of individual genes from oligonucleotides, a shuffling of protein domains in order to create novel biocatalysts, the assembly of multiple enzyme encoding genes in metabolic pathway design, or strain development at the production stage. The CoLibry concept has been designed in order to close the gap between recombinant production of individual genes and genome editing.},
  language  = {de}
}
@article{MuschallikMolinnusBongaertsetal.2017,
  author    = {Muschallik, Lukas and Molinnus, Denise and Bongaerts, Johannes and Pohl, Martina and Wagner, Torsten and Sch{\"o}ning, Michael Josef and Siegert, Petra and Selmer, Thorsten},
  title     = {(R,R)-Butane-2,3-diol Dehydrogenase from Bacillus clausii DSM 8716T: Cloning and Expression of the bdhA-Gene, and Initial Characterization of Enzyme},
  series = {Journal of Biotechnology},
  volume    = {258},
  journal   = {Journal of Biotechnology},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {0168-1656},
  doi       = {10.1016/j.jbiotec.2017.07.020},
  pages     = {41 -- 50},
  year      = {2017},
  abstract  = {The gene encoding a putative (R,R)-butane-2,3-diol dehydrogenase (bdhA) from Bacillus clausii DSM 8716T was isolated, sequenced and expressed in Escherichia coli. The amino acid sequence of the encoded protein is only distantly related to previously studied enzymes (identity 33-43\%) and exhibited some uncharted peculiarities. An N-terminally StrepII-tagged enzyme variant was purified and initially characterized. The isolated enzyme catalyzed the (R)-specific oxidation of (R,R)- and meso-butane-2,3-diol to (R)- and (S)-acetoin with specific activities of 12 U/mg and 23 U/mg, respectively. Likewise, racemic acetoin was reduced with a specific activity of up to 115 U/mg yielding a mixture of (R,R)- and meso-butane-2,3-diol, while the enzyme reduced butane-2,3-dione (Vmax 74 U/mg) solely to (R,R)-butane-2,3-diol via (R)-acetoin. For these reactions only activity with the co-substrates NADH/NAD+ was observed. The enzyme accepted a selection of vicinal diketones, α-hydroxy ketones and vicinal diols as alternative substrates. Although the physiological function of the enzyme in B. clausii remains elusive, the data presented herein clearly demonstrates that the encoded enzyme is a genuine (R,R)-butane-2,3-diol dehydrogenase with potential for applications in biocatalysis and sensor development.},
  language  = {en}
}
@article{RoehlenPilasSchoeningetal.2017,
  author    = {R{\"o}hlen, Desiree and Pilas, Johanna and Sch{\"o}ning, Michael Josef and Selmer, Thorsten},
  title     = {Development of an amperometric biosensor platform for the combined determination of l-Malic, Fumaric, and l-Aspartic acid},
  series = {Applied Biochemistry and Biotechnology},
  volume    = {183},
  journal   = {Applied Biochemistry and Biotechnology},
  publisher = {Springer},
  address   = {Berlin},
  issn      = {1559-0291},
  doi       = {10.1007/s12010-017-2578-1},
  pages     = {566 -- 581},
  year      = {2017},
  abstract  = {Three amperometric biosensors have been developed for the detection of L-malic acid, fumaric acid, and L -aspartic acid, all based on the combination of a malate-specific dehydrogenase (MDH, EC 1.1.1.37) and diaphorase (DIA, EC 1.8.1.4). The stepwise expansion of the malate platform with the enzymes fumarate hydratase (FH, EC 4.2.1.2) and aspartate ammonia-lyase (ASPA, EC 4.3.1.1) resulted in multi-enzyme reaction cascades and, thus, augmentation of the substrate spectrum of the sensors. Electrochemical measurements were carried out in presence of the cofactor β-nicotinamide adenine dinucleotide (NAD+) and the redox mediator hexacyanoferrate (III) (HCFIII). The amperometric detection is mediated by oxidation of hexacyanoferrate (II) (HCFII) at an applied potential of + 0.3 V vs. Ag/AgCl. For each biosensor, optimum working conditions were defined by adjustment of cofactor concentrations, buffer pH, and immobilization procedure. Under these improved conditions, amperometric responses were linear up to 3.0 mM for L-malate and fumarate, respectively, with a corresponding sensitivity of 0.7 μA mM-1 (L-malate biosensor) and 0.4 μA mM-1 (fumarate biosensor). The L-aspartate detection system displayed a linear range of 1.0-10.0 mM with a sensitivity of 0.09 μA mM-1. The sensor characteristics suggest that the developed platform provides a promising method for the detection and differentiation of the three substrates.},
  language  = {en}
}
@article{PilasYaziciSelmeretal.2017,
  author    = {Pilas, Johanna and Yazici, Yasemen and Selmer, Thorsten and Keusgen, Michael and Sch{\"o}ning, Michael Josef},
  title     = {Optimization of an amperometric biosensor array for simultaneous measurement of ethanol, formate, d- and l-lactate},
  series = {Electrochimica Acta},
  volume    = {251},
  journal   = {Electrochimica Acta},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {0013-4686},
  doi       = {10.1016/j.electacta.2017.07.119},
  pages     = {256 -- 262},
  year      = {2017},
  abstract  = {The immobilization of NAD+-dependent dehydrogenases, in combination with a diaphorase, enables the facile development of multiparametric sensing devices. In this work, an amperometric biosensor array for simultaneous determination of ethanol, formate, d- and l-lactate is presented. Enzyme immobilization on platinum thin-film electrodes was realized by chemical cross-linking with glutaraldehyde. The optimization of the sensor performance was investigated with regard to enzyme loading, glutaraldehyde concentration, pH, cofactor concentration and temperature. Under optimal working conditions (potassium phosphate buffer with pH 7.5, 2.5 mmol L-1 NAD+, 2.0 mmol L-1 ferricyanide, 25 °C and 0.4\% glutaraldehyde) the linear working range and sensitivity of the four sensor elements was improved. Simultaneous and cross-talk free measurements of four different metabolic parameters were performed successfully. The reliable analytical performance of the biosensor array was demonstrated by application in a clarified sample of inoculum sludge. Thereby, a promising approach for on-site monitoring of fermentation processes is provided.},
  language  = {en}
}