@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{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{HuckSchiffelsHerreraetal.2013,
  author    = {Huck, Christina and Schiffels, Johannes and Herrera, Cony N. and Schelden, Maximilian and Selmer, Thorsten and Poghossian, Arshak and Baumann, Marcus and Wagner, Patrick and Sch{\"o}ning, Michael Josef},
  title     = {Metabolic responses of Escherichia coli upon glucose pulses captured by a capacitive field-effect sensor},
  series = {Physica Status Solidi (A)},
  volume    = {210},
  journal   = {Physica Status Solidi (A)},
  number    = {5},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {0031-8965},
  doi       = {10.1002/pssa.201200900},
  pages     = {926 -- 931},
  year      = {2013},
  abstract  = {Living cells are complex biological systems transforming metabolites taken up from the surrounding medium. Monitoring the responses of such cells to certain substrate concentrations is a challenging task and offers possibilities to gain insight into the vitality of a community influenced by the growth environment. Cell-based sensors represent a promising platform for monitoring the metabolic activity and thus, the "welfare" of relevant organisms. In the present study, metabolic responses of the model bacterium Escherichia coli in suspension, layered onto a capacitive field-effect structure, were examined to pulses of glucose in the concentration range between 0.05 and 2 mM. It was found that acidification of the surrounding medium takes place immediately after glucose addition and follows Michaelis-Menten kinetic behavior as a function of the glucose concentration. In future, the presented setup can, therefore, be used to study substrate specificities on the enzymatic level and may as well be used to perform investigations of more complex metabolic responses. Conclusions and perspectives highlighting this system are discussed.},
  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{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}
}